title: Two-dimensional vibrational optical probes for peptide fast folding investigation.
abstract: A simulation study shows that early protein folding events may be investigated by using a recently developed family of nonlinear infrared techniques that combine the high temporal and spatial resolution of multidimensional spectroscopy with the chirality-specific sensitivity of amide vibrations to structure. We demonstrate how the structural sensitivity of cross-peaks in two-dimensional correlation plots of chiral signals of an alpha helix and a beta hairpin may be used to clearly resolve structural and dynamical details undetectable by one-dimensional techniques (e.g. circular dichroism) and identify structures indistinguishable by NMR.
authors.affiliation: Department of Chemistry, University of California, Irvine, CA 92697, USA.
authors.forename: Wei
authors.initials: W
authors.lastname: Zhuang
authors.forename: Darius
authors.initials: D
authors.lastname: Abramavicius
authors.forename: Shaul
authors.initials: S
authors.lastname: Mukamel
mesh_terms: D003198:Computer Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D013237:Stereoisomerism; D013997:Time Factors; D014732:Vibration
chemical_list: D010455:Peptides