Abstract

Infrared (IR) vibrational scattering scanning near-field optical microscopy (s-SNOM) has advanced to become a powerful nanoimaging and spectroscopy technique with applications ranging from biological to quantum materials. However, full spatiospectral s-SNOM continues to be challenged by long measurement times and drift during the acquisition of large associated datasets. Here, we demonstrate a novel approach of computational spatiospectral s-SNOM by transforming the basis from the stationary frame into the rotating frame of the IR carrier frequency. We demonstrate an acceleration of IR s-SNOM data collection by a factor of 10 or more in combination with prior knowledge of the electronic or vibrational resonances to be probed, the IR source excitation spectrum, and other general sample characteristics. As an example, we apply rotating-frame s-SNOM (R-sSNOM) to chemical nanoimaging of ultrathin protein sheets in a mollusk shell. R-sSNOM enables high-voxel-density imaging of sparsely distributed molecules in an extended matrix. It is generally applicable to many multiscale material systems with sparse features and can be extended to other spectroscopic nanoimaging modalities.

© 2019 Optical Society of America under the terms of the OSA Open Access Publishing Agreement

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    [Crossref]
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    [Crossref]
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    [Crossref]
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2018 (2)

O. Khatib, H. A. Bechtel, M. C. Martin, M. B. Raschke, and G. L. Carr, “Far infrared synchrotron near-field nanoimaging and nanospectroscopy,” ACS Photon. 5, 2773–2779 (2018).
[Crossref]

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
[Crossref]

2017 (1)

I. Amenabar, S. Poly, M. Goikoetxea, W. Nuansing, P. Lasch, and R. Hillenbrand, “Hyperspectral infrared nanoimaging of organic samples based on Fourier transform infrared nanospectroscopy,” Nat. Commun. 8, 14402 (2017).
[Crossref]

2016 (2)

2015 (1)

E. A. Muller, B. Pollard, and M. B. Raschke, “Infrared chemical nanoimaging: accessing structure, coupling, and dynamics on molecular length scales,” J. Phys. Chem. Lett. 6, 1275–1284 (2015).
[Crossref]

2014 (1)

H. A. Bechtel, E. A. Muller, R. L. Olmon, M. C. Martin, and M. B. Raschke, “Ultrabroadband infrared nanospectroscopic imaging,” Proc. Natl. Acad. Sci. USA 111, 7191–7196 (2014).
[Crossref]

2013 (3)

I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
[Crossref]

S. Berweger, D. M. Nguyen, E. A. Muller, H. A. Bechtel, T. T. Perkins, and M. B. Raschke, “Nano-chemical infrared imaging of membrane proteins in lipid bilayers,” J. Am. Chem. Soc. 135, 18292–18295(2013).
[Crossref]

Y. Dauphin, A. D. Ball, H. Castillo-Michel, C. Chevallard, J.-P. Cuif, B. Farre, S. Pouvreau, and M. Salomé, “In situ distribution and characterization of the organic content of the oyster shell Crassostrea gigas (Mollusca, Bivalvia),” Micron 44, 373–383 (2013).
[Crossref]

2012 (5)

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
[Crossref]

F. Marin, N. Le Roy, and B. Marie, “The formation and mineralization of mollusk shell,” Front. Biosci. S4, 1099–1125 (2012).
[Crossref]

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

J. M. Atkin, S. Berweger, A. C. Jones, and M. B. Raschke, “Nano-optical imaging and spectroscopy of order, phases, and domains in complex solids,” Adv. Phys. 61, 745–842 (2012).
[Crossref]

S. K. Karthick Kumar, A. Tamimi, and M. D. Fayer, “Comparisons of 2D IR measured spectral diffusion in rotating frames using pulse shaping and in the stationary frame using the standard method,” J. Chem. Phys. 137, 184201 (2012).
[Crossref]

2011 (2)

B. Farre, A. Brunelle, O. Laprévote, J.-P. Cuif, C. T. Williams, and Y. Dauphin, “Shell layers of the black-lip pearl oyster Pinctada margaritifera: matching microstructure and composition,” Comp. Biochem. Physiol. Part B 159, 131–139 (2011).
[Crossref]

B. Marie, I. Zanella-Cléon, N. Guichard, M. Becchi, and F. Marin, “Novel proteins from the calcifying shell matrix of the pacific oyster Crassostrea gigas,” Mar. Biotechnol. 13, 1159–1168 (2011).
[Crossref]

2009 (1)

S.-H. Shim and M. T. Zanni, “How to turn your pump–probe instrument into a multidimensional spectrometer: 2D IR and Vis spectroscopies via pulse shaping,” Phys. Chem. Chem. Phys. 11, 748–761(2009).
[Crossref]

2007 (3)

F. Marin, G. Luquet, B. Marie, and D. Medakovic, “Molluscan shell proteins: primary structure, origin, and evolution,” Curr. Top. Dev. Biol. 80, 209–276 (2007).
[Crossref]

F. Marin, B. Pokroy, G. Luquet, P. Layrolle, and K. De Groot, “Protein mapping of calcium carbonate biominerals by immunogold,” Biomaterials 28, 2368–2377 (2007).
[Crossref]

M. Abe, Y. Sugimoto, T. Namikawa, K. Morita, N. Oyabu, and S. Morita, “Drift-compensated data acquisition performed at room temperature with frequency modulation atomic force microscopy,” Appl. Phys. Lett. 90, 203103 (2007).
[Crossref]

2006 (1)

M. Brehm, T. Taubner, R. Hillenbrand, and F. Keilmann, “Infrared spectroscopic mapping of single nanoparticles and viruses at nanoscale resolution,” Nano Lett. 6, 1307–1310 (2006).
[Crossref]

2003 (3)

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Y. Dauphin, “Soluble organic matrices of the calcitic prismatic shell layers of two pteriomorphid bivalves,” J. Biol. Chem. 278, 15168–15177 (2003).
[Crossref]

Y. Dauphin, J.-P. Cuif, J. Doucet, M. Salom, J. Susini, and C. T. Willams, “In situ chemical speciation of sulfur in calcitic biominerals and the simple prism concept,” J. Struct. Biol. 142, 272–280 (2003).
[Crossref]

2002 (1)

C. Scheurer and S. Mukamel, “Magnetic resonance analogies in multidimensional vibrational spectroscopy,” Bull. Chem. Soc. Jpn. 75, 989–999 (2002).
[Crossref]

1999 (1)

A. W. Albrecht, J. D. Hybl, S. M. G. Faeder, and D. M. Jonas, “Experimental distinction between phase shifts and time delays: implications for femtosecond spectroscopy and coherent control of chemical reactions,” J. Chem. Phys. 111, 10934–10956 (1999).
[Crossref]

1954 (1)

I. Rabi, N. Ramsey, and J. Schwinger, “Use of rotating coordinates in magnetic resonance problems,” Rev. Mod. Phys. 26, 167–171 (1954).
[Crossref]

Abe, M.

M. Abe, Y. Sugimoto, T. Namikawa, K. Morita, N. Oyabu, and S. Morita, “Drift-compensated data acquisition performed at room temperature with frequency modulation atomic force microscopy,” Appl. Phys. Lett. 90, 203103 (2007).
[Crossref]

Aggarwal, I. D.

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Albrecht, A. W.

A. W. Albrecht, J. D. Hybl, S. M. G. Faeder, and D. M. Jonas, “Experimental distinction between phase shifts and time delays: implications for femtosecond spectroscopy and coherent control of chemical reactions,” J. Chem. Phys. 111, 10934–10956 (1999).
[Crossref]

Alonso-González, P.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Amenabar, I.

I. Amenabar, S. Poly, M. Goikoetxea, W. Nuansing, P. Lasch, and R. Hillenbrand, “Hyperspectral infrared nanoimaging of organic samples based on Fourier transform infrared nanospectroscopy,” Nat. Commun. 8, 14402 (2017).
[Crossref]

I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
[Crossref]

Atkin, J. M.

J. M. Atkin, S. Berweger, A. C. Jones, and M. B. Raschke, “Nano-optical imaging and spectroscopy of order, phases, and domains in complex solids,” Adv. Phys. 61, 745–842 (2012).
[Crossref]

Badioli, M.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Ball, A. D.

Y. Dauphin, A. D. Ball, H. Castillo-Michel, C. Chevallard, J.-P. Cuif, B. Farre, S. Pouvreau, and M. Salomé, “In situ distribution and characterization of the organic content of the oyster shell Crassostrea gigas (Mollusca, Bivalvia),” Micron 44, 373–383 (2013).
[Crossref]

Becchi, M.

B. Marie, I. Zanella-Cléon, N. Guichard, M. Becchi, and F. Marin, “Novel proteins from the calcifying shell matrix of the pacific oyster Crassostrea gigas,” Mar. Biotechnol. 13, 1159–1168 (2011).
[Crossref]

Bechtel, H. A.

O. Khatib, H. A. Bechtel, M. C. Martin, M. B. Raschke, and G. L. Carr, “Far infrared synchrotron near-field nanoimaging and nanospectroscopy,” ACS Photon. 5, 2773–2779 (2018).
[Crossref]

H. A. Bechtel, E. A. Muller, R. L. Olmon, M. C. Martin, and M. B. Raschke, “Ultrabroadband infrared nanospectroscopic imaging,” Proc. Natl. Acad. Sci. USA 111, 7191–7196 (2014).
[Crossref]

S. Berweger, D. M. Nguyen, E. A. Muller, H. A. Bechtel, T. T. Perkins, and M. B. Raschke, “Nano-chemical infrared imaging of membrane proteins in lipid bilayers,” J. Am. Chem. Soc. 135, 18292–18295(2013).
[Crossref]

Belliard, C.

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
[Crossref]

Berweger, S.

S. Berweger, D. M. Nguyen, E. A. Muller, H. A. Bechtel, T. T. Perkins, and M. B. Raschke, “Nano-chemical infrared imaging of membrane proteins in lipid bilayers,” J. Am. Chem. Soc. 135, 18292–18295(2013).
[Crossref]

J. M. Atkin, S. Berweger, A. C. Jones, and M. B. Raschke, “Nano-optical imaging and spectroscopy of order, phases, and domains in complex solids,” Adv. Phys. 61, 745–842 (2012).
[Crossref]

Bittner, A. M.

I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
[Crossref]

Brehm, M.

M. Brehm, T. Taubner, R. Hillenbrand, and F. Keilmann, “Infrared spectroscopic mapping of single nanoparticles and viruses at nanoscale resolution,” Nano Lett. 6, 1307–1310 (2006).
[Crossref]

Brunelle, A.

B. Farre, A. Brunelle, O. Laprévote, J.-P. Cuif, C. T. Williams, and Y. Dauphin, “Shell layers of the black-lip pearl oyster Pinctada margaritifera: matching microstructure and composition,” Comp. Biochem. Physiol. Part B 159, 131–139 (2011).
[Crossref]

Camara, N.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Carr, G. L.

O. Khatib, H. A. Bechtel, M. C. Martin, M. B. Raschke, and G. L. Carr, “Far infrared synchrotron near-field nanoimaging and nanospectroscopy,” ACS Photon. 5, 2773–2779 (2018).
[Crossref]

Carter, G. J.

G. J. Carter, “Guide to bivalve shell microstructures,” in Skeletal Growth of Aquatic Organisms (Plenum Press, 1980), pp. 645–673.

Castillo-Michel, H.

Y. Dauphin, A. D. Ball, H. Castillo-Michel, C. Chevallard, J.-P. Cuif, B. Farre, S. Pouvreau, and M. Salomé, “In situ distribution and characterization of the organic content of the oyster shell Crassostrea gigas (Mollusca, Bivalvia),” Micron 44, 373–383 (2013).
[Crossref]

Centeno, A.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Chen, J.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Chevallard, C.

Y. Dauphin, A. D. Ball, H. Castillo-Michel, C. Chevallard, J.-P. Cuif, B. Farre, S. Pouvreau, and M. Salomé, “In situ distribution and characterization of the organic content of the oyster shell Crassostrea gigas (Mollusca, Bivalvia),” Micron 44, 373–383 (2013).
[Crossref]

Cochennec-Laureau, N.

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
[Crossref]

Congiu-Castellano, A.

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Cricenti, A.

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B. Farre, A. Brunelle, O. Laprévote, J.-P. Cuif, C. T. Williams, and Y. Dauphin, “Shell layers of the black-lip pearl oyster Pinctada margaritifera: matching microstructure and composition,” Comp. Biochem. Physiol. Part B 159, 131–139 (2011).
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Y. Dauphin, J.-P. Cuif, J. Doucet, M. Salom, J. Susini, and C. T. Willams, “In situ chemical speciation of sulfur in calcitic biominerals and the simple prism concept,” J. Struct. Biol. 142, 272–280 (2003).
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J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
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Faeder, S. M. G.

A. W. Albrecht, J. D. Hybl, S. M. G. Faeder, and D. M. Jonas, “Experimental distinction between phase shifts and time delays: implications for femtosecond spectroscopy and coherent control of chemical reactions,” J. Chem. Phys. 111, 10934–10956 (1999).
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Farre, B.

Y. Dauphin, A. D. Ball, H. Castillo-Michel, C. Chevallard, J.-P. Cuif, B. Farre, S. Pouvreau, and M. Salomé, “In situ distribution and characterization of the organic content of the oyster shell Crassostrea gigas (Mollusca, Bivalvia),” Micron 44, 373–383 (2013).
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B. Farre, A. Brunelle, O. Laprévote, J.-P. Cuif, C. T. Williams, and Y. Dauphin, “Shell layers of the black-lip pearl oyster Pinctada margaritifera: matching microstructure and composition,” Comp. Biochem. Physiol. Part B 159, 131–139 (2011).
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S. K. Karthick Kumar, A. Tamimi, and M. D. Fayer, “Comparisons of 2D IR measured spectral diffusion in rotating frames using pulse shaping and in the stationary frame using the standard method,” J. Chem. Phys. 137, 184201 (2012).
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B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
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B. Pollard, F. C. B. Maia, M. B. Raschke, and R. O. Freitas, “Infrared vibrational nanospectroscopy by self-referenced interferometry,” Nano Lett. 16, 55–61 (2016).
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A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
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Godignon, P.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
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Goikoetxea, M.

I. Amenabar, S. Poly, M. Goikoetxea, W. Nuansing, P. Lasch, and R. Hillenbrand, “Hyperspectral infrared nanoimaging of organic samples based on Fourier transform infrared nanospectroscopy,” Nat. Commun. 8, 14402 (2017).
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I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
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B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
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Guichard, N.

B. Marie, I. Zanella-Cléon, N. Guichard, M. Becchi, and F. Marin, “Novel proteins from the calcifying shell matrix of the pacific oyster Crassostrea gigas,” Mar. Biotechnol. 13, 1159–1168 (2011).
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I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
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B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
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Hillenbrand, R.

I. Amenabar, S. Poly, M. Goikoetxea, W. Nuansing, P. Lasch, and R. Hillenbrand, “Hyperspectral infrared nanoimaging of organic samples based on Fourier transform infrared nanospectroscopy,” Nat. Commun. 8, 14402 (2017).
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I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
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J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

M. Brehm, T. Taubner, R. Hillenbrand, and F. Keilmann, “Infrared spectroscopic mapping of single nanoparticles and viruses at nanoscale resolution,” Nano Lett. 6, 1307–1310 (2006).
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B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
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Hornemann, A.

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
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I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
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I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
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J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
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A. W. Albrecht, J. D. Hybl, S. M. G. Faeder, and D. M. Jonas, “Experimental distinction between phase shifts and time delays: implications for femtosecond spectroscopy and coherent control of chemical reactions,” J. Chem. Phys. 111, 10934–10956 (1999).
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Javier García De Abajo, F.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
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B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
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A. W. Albrecht, J. D. Hybl, S. M. G. Faeder, and D. M. Jonas, “Experimental distinction between phase shifts and time delays: implications for femtosecond spectroscopy and coherent control of chemical reactions,” J. Chem. Phys. 111, 10934–10956 (1999).
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Karthick Kumar, S. K.

S. K. Karthick Kumar, A. Tamimi, and M. D. Fayer, “Comparisons of 2D IR measured spectral diffusion in rotating frames using pulse shaping and in the stationary frame using the standard method,” J. Chem. Phys. 137, 184201 (2012).
[Crossref]

Kästner, B.

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
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M. Brehm, T. Taubner, R. Hillenbrand, and F. Keilmann, “Infrared spectroscopic mapping of single nanoparticles and viruses at nanoscale resolution,” Nano Lett. 6, 1307–1310 (2006).
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Khatib, O.

O. Khatib, H. A. Bechtel, M. C. Martin, M. B. Raschke, and G. L. Carr, “Far infrared synchrotron near-field nanoimaging and nanospectroscopy,” ACS Photon. 5, 2773–2779 (2018).
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Knez, M.

I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
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J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
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Kramer, P. L.

Kruskopf, M.

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
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I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
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Laprévote, O.

B. Farre, A. Brunelle, O. Laprévote, J.-P. Cuif, C. T. Williams, and Y. Dauphin, “Shell layers of the black-lip pearl oyster Pinctada margaritifera: matching microstructure and composition,” Comp. Biochem. Physiol. Part B 159, 131–139 (2011).
[Crossref]

Lasch, P.

I. Amenabar, S. Poly, M. Goikoetxea, W. Nuansing, P. Lasch, and R. Hillenbrand, “Hyperspectral infrared nanoimaging of organic samples based on Fourier transform infrared nanospectroscopy,” Nat. Commun. 8, 14402 (2017).
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Layrolle, P.

F. Marin, B. Pokroy, G. Luquet, P. Layrolle, and K. De Groot, “Protein mapping of calcium carbonate biominerals by immunogold,” Biomaterials 28, 2368–2377 (2007).
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Le Roy, N.

F. Marin, N. Le Roy, and B. Marie, “The formation and mineralization of mollusk shell,” Front. Biosci. S4, 1099–1125 (2012).
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A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
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F. Marin, B. Pokroy, G. Luquet, P. Layrolle, and K. De Groot, “Protein mapping of calcium carbonate biominerals by immunogold,” Biomaterials 28, 2368–2377 (2007).
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F. Marin, G. Luquet, B. Marie, and D. Medakovic, “Molluscan shell proteins: primary structure, origin, and evolution,” Curr. Top. Dev. Biol. 80, 209–276 (2007).
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Maia, F. C. B.

B. Pollard, F. C. B. Maia, M. B. Raschke, and R. O. Freitas, “Infrared vibrational nanospectroscopy by self-referenced interferometry,” Nano Lett. 16, 55–61 (2016).
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Margaritondo, G.

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
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Marie, B.

F. Marin, N. Le Roy, and B. Marie, “The formation and mineralization of mollusk shell,” Front. Biosci. S4, 1099–1125 (2012).
[Crossref]

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
[Crossref]

B. Marie, I. Zanella-Cléon, N. Guichard, M. Becchi, and F. Marin, “Novel proteins from the calcifying shell matrix of the pacific oyster Crassostrea gigas,” Mar. Biotechnol. 13, 1159–1168 (2011).
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F. Marin, G. Luquet, B. Marie, and D. Medakovic, “Molluscan shell proteins: primary structure, origin, and evolution,” Curr. Top. Dev. Biol. 80, 209–276 (2007).
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Marin, F.

F. Marin, N. Le Roy, and B. Marie, “The formation and mineralization of mollusk shell,” Front. Biosci. S4, 1099–1125 (2012).
[Crossref]

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
[Crossref]

B. Marie, I. Zanella-Cléon, N. Guichard, M. Becchi, and F. Marin, “Novel proteins from the calcifying shell matrix of the pacific oyster Crassostrea gigas,” Mar. Biotechnol. 13, 1159–1168 (2011).
[Crossref]

F. Marin, G. Luquet, B. Marie, and D. Medakovic, “Molluscan shell proteins: primary structure, origin, and evolution,” Curr. Top. Dev. Biol. 80, 209–276 (2007).
[Crossref]

F. Marin, B. Pokroy, G. Luquet, P. Layrolle, and K. De Groot, “Protein mapping of calcium carbonate biominerals by immunogold,” Biomaterials 28, 2368–2377 (2007).
[Crossref]

Martin, M. C.

O. Khatib, H. A. Bechtel, M. C. Martin, M. B. Raschke, and G. L. Carr, “Far infrared synchrotron near-field nanoimaging and nanospectroscopy,” ACS Photon. 5, 2773–2779 (2018).
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H. A. Bechtel, E. A. Muller, R. L. Olmon, M. C. Martin, and M. B. Raschke, “Ultrabroadband infrared nanospectroscopic imaging,” Proc. Natl. Acad. Sci. USA 111, 7191–7196 (2014).
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Medakovic, D.

F. Marin, G. Luquet, B. Marie, and D. Medakovic, “Molluscan shell proteins: primary structure, origin, and evolution,” Curr. Top. Dev. Biol. 80, 209–276 (2007).
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Montagnani, C.

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
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M. Abe, Y. Sugimoto, T. Namikawa, K. Morita, N. Oyabu, and S. Morita, “Drift-compensated data acquisition performed at room temperature with frequency modulation atomic force microscopy,” Appl. Phys. Lett. 90, 203103 (2007).
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H. A. Bechtel, E. A. Muller, R. L. Olmon, M. C. Martin, and M. B. Raschke, “Ultrabroadband infrared nanospectroscopic imaging,” Proc. Natl. Acad. Sci. USA 111, 7191–7196 (2014).
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S. Berweger, D. M. Nguyen, E. A. Muller, H. A. Bechtel, T. T. Perkins, and M. B. Raschke, “Nano-chemical infrared imaging of membrane proteins in lipid bilayers,” J. Am. Chem. Soc. 135, 18292–18295(2013).
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S. Berweger, D. M. Nguyen, E. A. Muller, H. A. Bechtel, T. T. Perkins, and M. B. Raschke, “Nano-chemical infrared imaging of membrane proteins in lipid bilayers,” J. Am. Chem. Soc. 135, 18292–18295(2013).
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I. Amenabar, S. Poly, M. Goikoetxea, W. Nuansing, P. Lasch, and R. Hillenbrand, “Hyperspectral infrared nanoimaging of organic samples based on Fourier transform infrared nanospectroscopy,” Nat. Commun. 8, 14402 (2017).
[Crossref]

I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
[Crossref]

Olmon, R. L.

H. A. Bechtel, E. A. Muller, R. L. Olmon, M. C. Martin, and M. B. Raschke, “Ultrabroadband infrared nanospectroscopic imaging,” Proc. Natl. Acad. Sci. USA 111, 7191–7196 (2014).
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Osmond, J.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Oyabu, N.

M. Abe, Y. Sugimoto, T. Namikawa, K. Morita, N. Oyabu, and S. Morita, “Drift-compensated data acquisition performed at room temperature with frequency modulation atomic force microscopy,” Appl. Phys. Lett. 90, 203103 (2007).
[Crossref]

Patoka, P.

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
[Crossref]

Perfetti, P.

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Perkins, T. T.

S. Berweger, D. M. Nguyen, E. A. Muller, H. A. Bechtel, T. T. Perkins, and M. B. Raschke, “Nano-chemical infrared imaging of membrane proteins in lipid bilayers,” J. Am. Chem. Soc. 135, 18292–18295(2013).
[Crossref]

Pesquera, A.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Pierz, K.

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
[Crossref]

Piquemal, D.

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
[Crossref]

Piston, D. W.

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Pokroy, B.

F. Marin, B. Pokroy, G. Luquet, P. Layrolle, and K. De Groot, “Protein mapping of calcium carbonate biominerals by immunogold,” Biomaterials 28, 2368–2377 (2007).
[Crossref]

Pollard, B.

B. Pollard, F. C. B. Maia, M. B. Raschke, and R. O. Freitas, “Infrared vibrational nanospectroscopy by self-referenced interferometry,” Nano Lett. 16, 55–61 (2016).
[Crossref]

E. A. Muller, B. Pollard, and M. B. Raschke, “Infrared chemical nanoimaging: accessing structure, coupling, and dynamics on molecular length scales,” J. Phys. Chem. Lett. 6, 1275–1284 (2015).
[Crossref]

Poly, S.

I. Amenabar, S. Poly, M. Goikoetxea, W. Nuansing, P. Lasch, and R. Hillenbrand, “Hyperspectral infrared nanoimaging of organic samples based on Fourier transform infrared nanospectroscopy,” Nat. Commun. 8, 14402 (2017).
[Crossref]

I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
[Crossref]

Pouvreau, S.

Y. Dauphin, A. D. Ball, H. Castillo-Michel, C. Chevallard, J.-P. Cuif, B. Farre, S. Pouvreau, and M. Salomé, “In situ distribution and characterization of the organic content of the oyster shell Crassostrea gigas (Mollusca, Bivalvia),” Micron 44, 373–383 (2013).
[Crossref]

Rabi, I.

I. Rabi, N. Ramsey, and J. Schwinger, “Use of rotating coordinates in magnetic resonance problems,” Rev. Mod. Phys. 26, 167–171 (1954).
[Crossref]

Ramsey, N.

I. Rabi, N. Ramsey, and J. Schwinger, “Use of rotating coordinates in magnetic resonance problems,” Rev. Mod. Phys. 26, 167–171 (1954).
[Crossref]

Raschke, M. B.

O. Khatib, H. A. Bechtel, M. C. Martin, M. B. Raschke, and G. L. Carr, “Far infrared synchrotron near-field nanoimaging and nanospectroscopy,” ACS Photon. 5, 2773–2779 (2018).
[Crossref]

B. Pollard, F. C. B. Maia, M. B. Raschke, and R. O. Freitas, “Infrared vibrational nanospectroscopy by self-referenced interferometry,” Nano Lett. 16, 55–61 (2016).
[Crossref]

E. A. Muller, B. Pollard, and M. B. Raschke, “Infrared chemical nanoimaging: accessing structure, coupling, and dynamics on molecular length scales,” J. Phys. Chem. Lett. 6, 1275–1284 (2015).
[Crossref]

H. A. Bechtel, E. A. Muller, R. L. Olmon, M. C. Martin, and M. B. Raschke, “Ultrabroadband infrared nanospectroscopic imaging,” Proc. Natl. Acad. Sci. USA 111, 7191–7196 (2014).
[Crossref]

S. Berweger, D. M. Nguyen, E. A. Muller, H. A. Bechtel, T. T. Perkins, and M. B. Raschke, “Nano-chemical infrared imaging of membrane proteins in lipid bilayers,” J. Am. Chem. Soc. 135, 18292–18295(2013).
[Crossref]

J. M. Atkin, S. Berweger, A. C. Jones, and M. B. Raschke, “Nano-optical imaging and spectroscopy of order, phases, and domains in complex solids,” Adv. Phys. 61, 745–842 (2012).
[Crossref]

Rizzo, M. A.

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Rü, E.

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
[Crossref]

Salom, M.

Y. Dauphin, J.-P. Cuif, J. Doucet, M. Salom, J. Susini, and C. T. Willams, “In situ chemical speciation of sulfur in calcitic biominerals and the simple prism concept,” J. Struct. Biol. 142, 272–280 (2003).
[Crossref]

Salomé, M.

Y. Dauphin, A. D. Ball, H. Castillo-Michel, C. Chevallard, J.-P. Cuif, B. Farre, S. Pouvreau, and M. Salomé, “In situ distribution and characterization of the organic content of the oyster shell Crassostrea gigas (Mollusca, Bivalvia),” Micron 44, 373–383 (2013).
[Crossref]

Sanghera, J. S.

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Scheurer, C.

C. Scheurer and S. Mukamel, “Magnetic resonance analogies in multidimensional vibrational spectroscopy,” Bull. Chem. Soc. Jpn. 75, 989–999 (2002).
[Crossref]

Schwinger, J.

I. Rabi, N. Ramsey, and J. Schwinger, “Use of rotating coordinates in magnetic resonance problems,” Rev. Mod. Phys. 26, 167–171 (1954).
[Crossref]

Shim, S.-H.

S.-H. Shim and M. T. Zanni, “How to turn your pump–probe instrument into a multidimensional spectrometer: 2D IR and Vis spectroscopies via pulse shaping,” Phys. Chem. Chem. Phys. 11, 748–761(2009).
[Crossref]

Sokolowsky, K. P.

Spasenovi, M.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Sugimoto, Y.

M. Abe, Y. Sugimoto, T. Namikawa, K. Morita, N. Oyabu, and S. Morita, “Drift-compensated data acquisition performed at room temperature with frequency modulation atomic force microscopy,” Appl. Phys. Lett. 90, 203103 (2007).
[Crossref]

Susini, J.

Y. Dauphin, J.-P. Cuif, J. Doucet, M. Salom, J. Susini, and C. T. Willams, “In situ chemical speciation of sulfur in calcitic biominerals and the simple prism concept,” J. Struct. Biol. 142, 272–280 (2003).
[Crossref]

Talley, D.

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Tamimi, A.

P. L. Kramer, C. H. Giammanco, A. Tamimi, D. J. Hoffman, K. P. Sokolowsky, and M. D. Fayer, “Quasi-rotating frame: accurate line shape determination with increased efficiency in noncollinear 2D optical spectroscopy,” J. Opt. Soc. Am. B 33, 1143–1156 (2016).
[Crossref]

S. K. Karthick Kumar, A. Tamimi, and M. D. Fayer, “Comparisons of 2D IR measured spectral diffusion in rotating frames using pulse shaping and in the stationary frame using the standard method,” J. Chem. Phys. 137, 184201 (2012).
[Crossref]

Taubner, T.

M. Brehm, T. Taubner, R. Hillenbrand, and F. Keilmann, “Infrared spectroscopic mapping of single nanoparticles and viruses at nanoscale resolution,” Nano Lett. 6, 1307–1310 (2006).
[Crossref]

Tayalé, A.

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
[Crossref]

Thongrattanasiri, S.

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Tolk, N. H.

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Ulm, G.

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
[Crossref]

Ulrich, G.

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
[Crossref]

Willams, C. T.

Y. Dauphin, J.-P. Cuif, J. Doucet, M. Salom, J. Susini, and C. T. Willams, “In situ chemical speciation of sulfur in calcitic biominerals and the simple prism concept,” J. Struct. Biol. 142, 272–280 (2003).
[Crossref]

Williams, C. T.

B. Farre, A. Brunelle, O. Laprévote, J.-P. Cuif, C. T. Williams, and Y. Dauphin, “Shell layers of the black-lip pearl oyster Pinctada margaritifera: matching microstructure and composition,” Comp. Biochem. Physiol. Part B 159, 131–139 (2011).
[Crossref]

Zanella-Cléon, I.

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
[Crossref]

B. Marie, I. Zanella-Cléon, N. Guichard, M. Becchi, and F. Marin, “Novel proteins from the calcifying shell matrix of the pacific oyster Crassostrea gigas,” Mar. Biotechnol. 13, 1159–1168 (2011).
[Crossref]

Zanni, M. T.

S.-H. Shim and M. T. Zanni, “How to turn your pump–probe instrument into a multidimensional spectrometer: 2D IR and Vis spectroscopies via pulse shaping,” Phys. Chem. Chem. Phys. 11, 748–761(2009).
[Crossref]

Zhang, L.

I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
[Crossref]

ACS Omega (1)

B. Kästner, C. M. Johnson, P. Hermann, M. Kruskopf, K. Pierz, A. Hoehl, A. Hornemann, G. Ulrich, J. Fehmel, P. Patoka, E. Rü, and G. Ulm, “Infrared nanospectroscopy of phospholipid and surfactin monolayer domains,” ACS Omega 3, 4141–4147 (2018).
[Crossref]

ACS Photon. (1)

O. Khatib, H. A. Bechtel, M. C. Martin, M. B. Raschke, and G. L. Carr, “Far infrared synchrotron near-field nanoimaging and nanospectroscopy,” ACS Photon. 5, 2773–2779 (2018).
[Crossref]

Adv. Phys. (1)

J. M. Atkin, S. Berweger, A. C. Jones, and M. B. Raschke, “Nano-optical imaging and spectroscopy of order, phases, and domains in complex solids,” Adv. Phys. 61, 745–842 (2012).
[Crossref]

Appl. Phys. Lett. (1)

M. Abe, Y. Sugimoto, T. Namikawa, K. Morita, N. Oyabu, and S. Morita, “Drift-compensated data acquisition performed at room temperature with frequency modulation atomic force microscopy,” Appl. Phys. Lett. 90, 203103 (2007).
[Crossref]

Biomaterials (1)

F. Marin, B. Pokroy, G. Luquet, P. Layrolle, and K. De Groot, “Protein mapping of calcium carbonate biominerals by immunogold,” Biomaterials 28, 2368–2377 (2007).
[Crossref]

Biophys. J. (1)

A. Cricenti, R. Generosi, M. Luce, P. Perfetti, G. Margaritondo, D. Talley, J. S. Sanghera, I. D. Aggarwal, N. H. Tolk, A. Congiu-Castellano, M. A. Rizzo, and D. W. Piston, “Chemically resolved imaging of biological cells and thin films by infrared scanning near-field optical microscopy,” Biophys. J. 85, 2705–2710 (2003).
[Crossref]

Bull. Chem. Soc. Jpn. (1)

C. Scheurer and S. Mukamel, “Magnetic resonance analogies in multidimensional vibrational spectroscopy,” Bull. Chem. Soc. Jpn. 75, 989–999 (2002).
[Crossref]

Comp. Biochem. Physiol. Part B (1)

B. Farre, A. Brunelle, O. Laprévote, J.-P. Cuif, C. T. Williams, and Y. Dauphin, “Shell layers of the black-lip pearl oyster Pinctada margaritifera: matching microstructure and composition,” Comp. Biochem. Physiol. Part B 159, 131–139 (2011).
[Crossref]

Curr. Top. Dev. Biol. (1)

F. Marin, G. Luquet, B. Marie, and D. Medakovic, “Molluscan shell proteins: primary structure, origin, and evolution,” Curr. Top. Dev. Biol. 80, 209–276 (2007).
[Crossref]

Front. Biosci. (1)

F. Marin, N. Le Roy, and B. Marie, “The formation and mineralization of mollusk shell,” Front. Biosci. S4, 1099–1125 (2012).
[Crossref]

J. Am. Chem. Soc. (1)

S. Berweger, D. M. Nguyen, E. A. Muller, H. A. Bechtel, T. T. Perkins, and M. B. Raschke, “Nano-chemical infrared imaging of membrane proteins in lipid bilayers,” J. Am. Chem. Soc. 135, 18292–18295(2013).
[Crossref]

J. Biol. Chem. (1)

Y. Dauphin, “Soluble organic matrices of the calcitic prismatic shell layers of two pteriomorphid bivalves,” J. Biol. Chem. 278, 15168–15177 (2003).
[Crossref]

J. Chem. Phys. (2)

A. W. Albrecht, J. D. Hybl, S. M. G. Faeder, and D. M. Jonas, “Experimental distinction between phase shifts and time delays: implications for femtosecond spectroscopy and coherent control of chemical reactions,” J. Chem. Phys. 111, 10934–10956 (1999).
[Crossref]

S. K. Karthick Kumar, A. Tamimi, and M. D. Fayer, “Comparisons of 2D IR measured spectral diffusion in rotating frames using pulse shaping and in the stationary frame using the standard method,” J. Chem. Phys. 137, 184201 (2012).
[Crossref]

J. Opt. Soc. Am. B (1)

J. Phys. Chem. Lett. (1)

E. A. Muller, B. Pollard, and M. B. Raschke, “Infrared chemical nanoimaging: accessing structure, coupling, and dynamics on molecular length scales,” J. Phys. Chem. Lett. 6, 1275–1284 (2015).
[Crossref]

J. Struct. Biol. (1)

Y. Dauphin, J.-P. Cuif, J. Doucet, M. Salom, J. Susini, and C. T. Willams, “In situ chemical speciation of sulfur in calcitic biominerals and the simple prism concept,” J. Struct. Biol. 142, 272–280 (2003).
[Crossref]

Mar. Biotechnol. (1)

B. Marie, I. Zanella-Cléon, N. Guichard, M. Becchi, and F. Marin, “Novel proteins from the calcifying shell matrix of the pacific oyster Crassostrea gigas,” Mar. Biotechnol. 13, 1159–1168 (2011).
[Crossref]

Micron (1)

Y. Dauphin, A. D. Ball, H. Castillo-Michel, C. Chevallard, J.-P. Cuif, B. Farre, S. Pouvreau, and M. Salomé, “In situ distribution and characterization of the organic content of the oyster shell Crassostrea gigas (Mollusca, Bivalvia),” Micron 44, 373–383 (2013).
[Crossref]

Nano Lett. (2)

B. Pollard, F. C. B. Maia, M. B. Raschke, and R. O. Freitas, “Infrared vibrational nanospectroscopy by self-referenced interferometry,” Nano Lett. 16, 55–61 (2016).
[Crossref]

M. Brehm, T. Taubner, R. Hillenbrand, and F. Keilmann, “Infrared spectroscopic mapping of single nanoparticles and viruses at nanoscale resolution,” Nano Lett. 6, 1307–1310 (2006).
[Crossref]

Nat. Commun. (2)

I. Amenabar, S. Poly, W. Nuansing, E. H. Hubrich, A. A. Govyadinov, F. Huth, R. Krutokhvostov, L. Zhang, M. Knez, J. Heberle, A. M. Bittner, and R. Hillenbrand, “Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy,” Nat. Commun. 4, 2890 (2013).
[Crossref]

I. Amenabar, S. Poly, M. Goikoetxea, W. Nuansing, P. Lasch, and R. Hillenbrand, “Hyperspectral infrared nanoimaging of organic samples based on Fourier transform infrared nanospectroscopy,” Nat. Commun. 8, 14402 (2017).
[Crossref]

Nature (1)

J. Chen, M. Badioli, P. Alonso-González, S. Thongrattanasiri, F. Huth, J. Osmond, M. Spasenovi, A. Centeno, A. Pesquera, P. Godignon, A. Z. Elorza, N. Camara, F. Javier García De Abajo, R. Hillenbrand, and F. H. L. Koppens, “Optical nano-imaging of gate-tunable graphene plasmons,” Nature 487, 77–81 (2012).
[Crossref]

Phys. Chem. Chem. Phys. (1)

S.-H. Shim and M. T. Zanni, “How to turn your pump–probe instrument into a multidimensional spectrometer: 2D IR and Vis spectroscopies via pulse shaping,” Phys. Chem. Chem. Phys. 11, 748–761(2009).
[Crossref]

Proc. Natl. Acad. Sci. USA (2)

H. A. Bechtel, E. A. Muller, R. L. Olmon, M. C. Martin, and M. B. Raschke, “Ultrabroadband infrared nanospectroscopic imaging,” Proc. Natl. Acad. Sci. USA 111, 7191–7196 (2014).
[Crossref]

B. Marie, C. Joubert, A. Tayalé, I. Zanella-Cléon, C. Belliard, D. Piquemal, N. Cochennec-Laureau, F. Marin, Y. Gueguen, and C. Montagnani, “Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell,” Proc. Natl. Acad. Sci. USA 109, 20986–20991 (2012).
[Crossref]

Rev. Mod. Phys. (1)

I. Rabi, N. Ramsey, and J. Schwinger, “Use of rotating coordinates in magnetic resonance problems,” Rev. Mod. Phys. 26, 167–171 (1954).
[Crossref]

Other (2)

J. Keeler, Understanding NMR Spectroscopy (Wiley, 2002).

G. J. Carter, “Guide to bivalve shell microstructures,” in Skeletal Growth of Aquatic Organisms (Plenum Press, 1980), pp. 645–673.

Supplementary Material (1)

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Figures (3)

Fig. 1.
Fig. 1. Rotating Frame s -SNOM (R-sSNOM). (a) Experimental design with an IR light source and asymmetric Michelson interferometer. (b) Schematic of rotating frame reducing the frequency of the basis waveforms (red and orange) to generate new waveforms (light and dark blue) with the same information, but with the beat frequency between the rotation and basis. (c) Depiction of resonant IR feature within the IR source bandwidth. (d) Full experimental nano-FTIR interferogram (red) and a 30x subsampled interferogram that is at the Nyquist limit (blue). (e) Low-frequency full dataset nano-FTIR interferogram rotated by 1550 cm 1 (red) and the similarly rotated subsampled points (blue). (f) Frequency comparison of stationary (red) and rotating frame (blue) spectral response.
Fig. 2.
Fig. 2. Rotating frame R-sSNOM imaging. (a) The prismatic layer (middle schematic, thickness exaggerated) surrounded by organic sheaths (right). (b) Near-field scattering amplitude heterodyne amplified at zero phase difference between tip and reference arms in the rotating frame and (c) stationary frame yielding lower spatial resolution of the same region compared with (b). The white dashed line emphasizes drift artifact. (d) Spatiospectral phase image of same region acquired with R-sSNOM. (e) Representative spectrum of location indicated in (d) showing typical amide I response of the organic sheath acquired with nano-FTIR (blue) and R-sSNOM (black).
Fig. 3.
Fig. 3. Spectral and Topographic Mapping. (a) Topography from AFM. (b) Strength of near-field phase response at 1680 cm 1 . (c) Correlation comparison of sample topography and amide phase response. Points of high value indicate high correlation, and points of low value indicate a deviation between topography and the local amide population (see color bar). (d) Correlation plot of height and phase dependence between (a) and (b) (see color bar).

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