Molecular Dynamics of Apo-Adenylate Kinase: A Distance Replica Exchange Method for the Free Energy of Conformational Fluctuations
Author:
Affiliation:
1. Department of Chemistry and the Quantitative Biology Modeling Initiative, Michigan State University, East Lansing, Michigan 48824-1322
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp064303c
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1. Induced-fit movements in adenylate kinases
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5. Multinuclear magnetic resonance studies of Escherichia coli adenylate kinase in free and bound forms . Resonance assignment, secondary structure and ligand binding
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