Abstract
The microscopic details of the protein dynamics in ligand binding to hemoglobin are not yet well understood. Much has been learned through study of the inverse problem, photodissociation of ligated hemoglobin. We have developed an apparatus to record transient IR vibrational spectra with 0.5-ps resolution.1 This technique has been applied to tracking the CO ligand dynamics during photodissociation of carboxyhemoglobin (HbCO) in water solution at room temperature.2
© 1989 Optical Society of America
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