Structural and thermodynamic characterization of allosteric transitions in human serum albumin with metadynamics simulations-Reference-Cited by-同舟云学术

Structural and thermodynamic characterization of allosteric transitions in human serum albumin with metadynamics simulations

Published:2024 Issue:7 Volume:26 Page:6436-6447
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Freire Thales Souza¹^ORCID,Zukerman-Schpector Julio²,Friedman Ran³^ORCID,Caracelli Ignez⁴

Affiliation:

1. Institute of Physics of the University of São Paulo, Department of General Physics, São Paulo-SP, Brazil

2. Department of Chemistry, Federal University of São Carlos, São Carlos-SP, Brazil

3. Department of Chemistry and Biomedical Sciences, Linnæus University, 391 82 Kalmar, Sweden

4. Department of Physics, Federal University of São Carlos, São Carlos-SP, Brazil

Abstract

Human serum albumin (HSA) is an allosteric protein that can change conformation state through low energy barriers, being the most prominent protein in blood plasma, responsible for the maintenance of blood viscosity and transport of endogenous and exogenous molecules.

Funder

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CP/D3CP04169G

Reference42 articles.

1. The Human Plasma Proteome

2. Human serum albumin: From bench to bedside

3. Allostery in a monomeric protein: The case of human serum albumin

4. Statistical Mechanics of Allosteric Enzymes

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