Related Experiment Video
Updated: May 7, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Two-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding
Hao Ren1, Zaizhi Lai, Jason D Biggs
1Department of Chemistry, University of California, Irvine, California 92697, USA. smukamel@uci.edu.
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.
Related Concept Videos
Raman Spectroscopy: Overview
However, a small fraction of the scattered light exhibits a frequency shift due to the exchange of energy between the incident photons and...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding Quality Check in the RER

