Ring Flips Revisited: 13C Relaxation Dispersion Measurements of Aromatic Side Chain Dynamics and Activation Barriers in Basic Pancreatic Trypsin Inhibitor
Author:
Affiliation:
1. Department of Biophysical Chemistry, Center for Molecular Protein Science, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden
Funder
Göran Gustafssons Stiftelse för Naturvetenskaplig och Medicinsk Forskning
Knut and Alice Wallenberg Foundation
Swedish Research Council
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi500462k
Reference44 articles.
1. Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI)
2. Dynamic model of globular protein conformations based on NMR studies in solution
3. Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance
4. Effect of Pressure on the Tertiary Structure and Dynamics of Folded Basic Pancreatic Trypsin Inhibitor
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