Two-dimensional vibrational optical probes for peptide fast folding investigation.
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.
Zhuang
Wei
W
Department of Chemistry, University of California, Irvine, CA 92697, USA.
Abramavicius
Darius
D
Mukamel
Shaul
S
D003198:Computer Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D013237:Stereoisomerism; D013997:Time Factors; D014732:Vibration
D010455:Peptides