Unperturbed Detection of the Dynamic Structure in the Hydrophobic Core of Trp-Cage via Two-Dimensional Infrared Spectroscopy
Author:
Affiliation:
1. Department of Chemistry, University of Nevada, Reno, Reno, Nevada 89557, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
General Materials Science,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.9b03706
Reference55 articles.
1. Designing a 20-residue protein
2. Smaller and Faster: The 20-Residue Trp-Cage Protein Folds in 4 μs
3. Understanding folding and design: Replica-exchange simulations of ``Trp-cage'' miniproteins
4. All-Atom Structure Prediction and Folding Simulations of a Stable Protein
5. The Trp Cage: Folding Kinetics and Unfolded State Topology via Molecular Dynamics Simulations
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