Free-Energy Landscape and Rate Estimation of the Aromatic Ring Flips in Basic Pancreatic Trypsin Inhibitors Using Metadynamics
Author:
Affiliation:
1. Division of Biophysical Chemistry, Lund University, Chemical Center, 22100 Lund, Sweden
Funder
Vetenskapsrådet
Publisher
American Chemical Society (ACS)
Subject
Physical and Theoretical Chemistry,Computer Science Applications
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.3c00460
Reference60 articles.
1. Clustering of low-energy conformations near the native structures of small proteins
2. A Sharp Thermal Transition of Fast Aromatic‐Ring Dynamics in Ubiquitin
3. Ring Flips Revisited: 13C Relaxation Dispersion Measurements of Aromatic Side Chain Dynamics and Activation Barriers in Basic Pancreatic Trypsin Inhibitor
4. NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor
5. Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI)
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