title: Two-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding.
abstract: We report a combined molecular dynamics (MD) and ab initio simulation study of the ultrafast broadband ultraviolet (UV) stimulated resonance Raman (SRR) spectra of the Trp-cage mini protein. Characteristic two dimensional (2D) SRR features of various folding states are identified. Structural fluctuations erode the cross peaks and the correlation between diagonal peaks is a good indicator of the α-helix formation.
authors.affiliation: Department of Chemistry, University of California, Irvine, California 92697, USA. smukamel@uci.edu.
authors.forename: Hao
authors.initials: H
authors.lastname: Ren
authors.forename: Zaizhi
authors.initials: Z
authors.lastname: Lai
authors.forename: Jason D
authors.initials: JD
authors.lastname: Biggs
authors.forename: Jin
authors.initials: J
authors.lastname: Wang
authors.forename: Shaul
authors.initials: S
authors.lastname: Mukamel
mesh_terms: D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011789:Quantum Theory; D013059:Spectrum Analysis, Raman; D013816:Thermodynamics; D014466:Ultraviolet Rays
chemical_list: D010455:Peptides; C508725:Trp-cage peptide