Abstract

Two dimensional ultraviolet (2DUV) spectra of protein backbone and side chains are simulated by a combined quantum mechanics (QM) and molecular mechanics (MM) protocol. The signals provide new insights into the protein structures, dynamics and functions. Simulated chirality-induced 2DUV spectra reveal characteristic patterns of protein secondary structures, and explore the structure and aggregation mechanism of amyloid fibrils which are associated with over 20 diseases related to protein misfolding. Signatures of aggregation propensity of peptides are identified

© 2011 Optical Society of America