Markov State Model of Solvent Features Reveals Water Dynamics in Protein-Peptide Binding
Author:
Affiliation:
1. Department of Chemistry, Temple University, Philadelphia, Pennsylvania 19122, United States
Funder
Army Research Laboratory
National Institute of General Medical Sciences
Division of Computer and Network Systems
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/acs.jpcb.3c04775
Reference57 articles.
1. Efficient Atomistic Simulation of Pathways and Calculation of Rate Constants for a Protein–Peptide Binding Process: Application to the MDM2 Protein and an Intrinsically Disordered p53 Peptide
2. Bridging Microscopic and Macroscopic Mechanisms of p53-MDM2 Binding with Kinetic Network Models
3. Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
4. Molecular Mechanism of the Interaction between MDM2 and p53
5. Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells
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