Structural Stability of Insulin Oligomers and Protein Association–Dissociation Processes: Free Energy Landscape and Universal Role of Water-Reference-Cited by-同舟云学术

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Structural Stability of Insulin Oligomers and Protein Association–Dissociation Processes: Free Energy Landscape and Universal Role of Water

Published:2021-10-22 Issue:43 Volume:125 Page:11793-11811
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Mukherjee Saumyak¹^ORCID,Acharya Subhajit¹,Mondal Sayantan¹^ORCID,Banerjee Puja¹,Bagchi Biman¹^ORCID

Affiliation:

1. Solid State and Structural Chemistry Unit, Indian Institute of Science, Bangalore 560012, India

Funder

Council of Scientific and Industrial Research

Science and Engineering Research Board

Indian Institute of Science

Department of Science and Technology, Ministry of Science and Technology

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.1c05811

Reference104 articles.

1. Kinetics of protein-protein association explained by Brownian dynamics computer simulation.

2. Brownian simulation of protein association and reaction

3. Dynamical control by water at a molecular level in protein dimer association and dissociation

4. Insulin dimer dissociation in aqueous solution: A computational study of free energy landscape and evolving microscopic structure along the reaction pathway

5. Mechanism of Solvent Control of Protein Dynamics

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