Insulin dimer dissociation in aqueous solution: A computational study of free energy landscape and evolving microscopic structure along the reaction pathway-Reference-Cited by-同舟云学术

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

Published:2018-09-21 Issue:11 Volume:149 Page:114902
ISSN:0021-9606
Container-title:The Journal of Chemical Physics
language:en
Short-container-title:The Journal of Chemical Physics

Author:

Banerjee Puja¹,Mondal Sayantan¹,Bagchi Biman¹^ORCID

Affiliation:

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

Funder

Sir J. C. Bose fellowship, DST , India

Department of Science and Technology, Ministry of Science and Technology

Council of Scientific and Industrial Research

University Grants Commission

Publisher

AIP Publishing

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://aip.scitation.org/doi/pdf/10.1063/1.5042290

Reference33 articles.

1. Protein topology determines binding mechanism

2. Symmetry and frustration in protein energy landscapes: A near degeneracy resolves the Rop dimer-folding mystery

3. Role of Water in Protein Aggregation and Amyloid Polymorphism

4. Toward a Molecular Theory of Early and Late Events in Monomer to Amyloid Fibril Formation

5. Insulin dimer dissociation and unfolding revealed by amide I two-dimensional infrared spectroscopy

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