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Two-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding

Published Web Location

https://doi.org/10.1039/c3cp51347e
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.

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