Thermally induced conformational changes and protein–protein interactions of bovine serum albumin in aqueous solution under different pH and ionic strengths as revealed by SAXS measurements-Reference-Cited by-同舟云学术

Thermally induced conformational changes and protein–protein interactions of bovine serum albumin in aqueous solution under different pH and ionic strengths as revealed by SAXS measurements

Published:2017 Issue:26 Volume:19 Page:17143-17155
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Molodenskiy Dmitry¹²³^ORCID,Shirshin Evgeny⁴⁵²³,Tikhonova Tatiana⁶⁵²³,Gruzinov Andrey¹²³,Peters Georgy¹²³,Spinozzi Francesco⁷⁸⁹¹⁰^ORCID

Affiliation:

1. National Research Centre “Kurchatov Institute”

2. Moscow

3. Russia

4. Department of Physics

5. M.V. Lomonosov Moscow State University

6. International Laser Center

7. Università Politecnica delle Marche

8. Dipartimento di Scienze della Vita e dell'Ambiente

9. Ancona

10. Italy

Abstract

Temperature-induced oligomerization of albumin before and after protein melting was studied using SAXS and interpreted in terms of interaction potential.

Funder

Russian Foundation for Basic Research

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CP/C6CP08809K

Reference73 articles.

1. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

2. Protein aggregation and neurodegenerative disease

3. The nature of the accessible and buried surfaces in proteins