biostudies-literatureRen HNIGMS NIH HHS19457-64https://www.ebi.ac.uk/biostudies/studies/S-EPMC3859311biostudies-literatureUnknown15(44)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.Physical chemistry chemical physics : PCCPTwo-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding.PMC3859311R01 GM-59230R01 GM059230Ren HBiggs JDLai ZMukamel SWang JfalseTwo-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding.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.2013-01-01T00:00:00Z2013 Nov2026-05-29T19:34:33.062Z2019-03-27T01:18:19ZS-EPMC38593112412663410.1039/c3cp51347e