Issue 44, 2013

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 ╬▒-helix formation.

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

Supplementary files

Article information

Article type
Paper
Submitted
29 Mar 2013
Accepted
11 Sep 2013
First published
20 Sep 2013

Phys. Chem. Chem. Phys., 2013,15, 19457-19464

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

H. Ren, Z. Lai, J. D. Biggs, J. Wang and S. Mukamel, Phys. Chem. Chem. Phys., 2013, 15, 19457 DOI: 10.1039/C3CP51347E

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