The effect of Ficoll 70 on thermally-induced and chemically-induced conformational transitions of an RTX protein is quantitatively accounted for by a unified excluded volume model-Reference-Cited by-同舟云学术

The effect of Ficoll 70 on thermally-induced and chemically-induced conformational transitions of an RTX protein is quantitatively accounted for by a unified excluded volume model

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

Author:

Chenal Alexandre¹^ORCID,Minton Allen P.²^ORCID

Affiliation:

1. Institut Pasteur, Université de Paris Cité, CNRS UMR3528, Biochemistry of Macromolecular Interactions Unit, F75015 Paris, France

2. Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA

Abstract

A unified excluded volume model based upon the effective hard particle approximation is developed and used to quantitatively model previously published experimental measurements of the effect of adding high concentrations of an “inert” polymer on conformational transitions of the toxin protein RCL.

Funder

Institut Pasteur

National Institute of Diabetes and Digestive and Kidney Diseases

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CP/D4CP02213K

Reference33 articles.

1. Molecular Crowding Stabilizes Both the Intrinsically Disordered Calcium-Free State and the Folded Calcium-Bound State of a Repeat in Toxin (RTX) Protein

2. Bordetella Adenylate Cyclase-Hemolysin Toxins

3. Structure–Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes

4. Calcium-dependent disorder-to-order transitions are central to the secretion and folding of the CyaA toxin of Bordetella pertussis, the causative agent of whooping cough