DESCRIPTION:
Probing the complex energy landscape, pathways and mechanisms of protein folding has been the subject of intense theoretical and experimental activity.Optical techniques have allowed the investigation of the formation of the basic peptide structural motiffs as well as fast-folding proteins and address critical questions such as what is the ultimate speed limit of the folding. However, fine details about correlations between different sections of the peptide (intramolecular) and between the peptide and solvent (intermolecular) are not readily available due to their low structural resolution. NMR techniques have much higher structural resolution but are limited to longer ( s) timescale. We show that early protein folding events may be investigated using a new family of nonlinear infrared techniques which combine the high temporal and spatial resolution of multidimensional spectroscopy with the chirality-specific sensitivity of amide vibrations to structure.
REFERENCE:
W. Zhuang, D. Abramavicius, T. Hayashi and S. Mukamel “Simulation
Protocols for Coherent Femtosecond Vibrational Spectra of Peptides” J.
Phys. Chem. B 2006, 110, 3362-3374.
W. Zhuang, D. Abramavicius, S. Mukamel “Novel Two-Dimensional Vibrational Optical Probes for Peptide Fast Folding Investigation” Proceedings of National Academy of Sciences.USA (In Press)