Hofmeister effects on protein stability are dependent on the nature of the unfolded state-Reference-Cited by-同舟云学术

Hofmeister effects on protein stability are dependent on the nature of the unfolded state

Published:2021 Issue:44 Volume:23 Page:25210-25225
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Ribeiro Sara S.¹^ORCID,Castro Tarsila G.²^ORCID,Gomes Cláudio M.³^ORCID,Marcos João C.¹^ORCID

Affiliation:

1. Centre of Chemistry, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal

2. Centre of Biological Engineering, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal

3. Biosystems and Integrative Sciences Institute, Faculdade de Ciências and Departamento de Química e Bioquímica, Universidade de Lisboa, 1749-016 Lisboa, Portugal

Abstract

The physico-chemical nature of the unfolded state determines the ion-specific Hofmeister effects on protein stability, namely the molecular interplay between ion-binding and surface tension effects.

Funder

Fundação para a Ciência e a Tecnologia

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2021/CP/D1CP02477A

Reference112 articles.

1. How Hofmeister ion interactions affect protein stability

2. Protein Stabilization and the Hofmeister Effect: The Role of Hydrophobic Solvation

3. Metal ions modulate the folding and stability of the tumor suppressor protein S100A2

4. Why Hofmeister effects of many salts favor protein folding but not DNA helix formation

5. Correlation of lysozyme activity and stability in the presence of Hofmeister series anions

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