Narrowing the gap between experimental and computational determination of methyl group dynamics in proteins
Author:
Affiliation:
1. Theoretical Chemistry
2. Ruhr-University Bochum
3. D-44780 Bochum
4. Germany
5. Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry
6. University of Aarhus
7. DK-8000 Aarhus
8. Denmark
Abstract
A synergistic analysis of methyl NMR relaxation data and MD simulations identifies ways to improve studies of protein dynamics.
Funder
Deutsche Forschungsgemeinschaft
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2018/CP/C8CP03915A
Reference90 articles.
1. Dynamic personalities of proteins
2. The Energy Landscapes and Motions of Proteins
3. Exposing the Moving Parts of Proteins with NMR Spectroscopy
4. Using NMR to study fast dynamics in proteins: methods and applications
5. New Tools Provide New Insights in NMR Studies of Protein Dynamics
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