Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin-Reference-Cited by-同舟云学术

Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin

Published:2020-09-02 Issue:20 Volume:594 Page:3293-3304
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Lett

Author:

Majorina Maria A.¹,Balobanov Vitaly A.¹,Uversky Vladimir N²³^ORCID,Melnik Bogdan S.¹^ORCID

Affiliation:

1. Institute of Protein research RAS Pushchino Russia

2. Department of Molecular Medicine and Byrd Alzheimer’s Research Institute Morsani College of Medicine University of South Florida Tampa FL USA

3. Institute for Biological Instrumentation of the Russian Academy of Sciences Federal Research Center “Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences” Pushchino, Moscow region Russia

Funder

Russian Foundation for Basic Research

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.13905

Reference34 articles.

1. Compactness of protein molten globules: temperature-induced structural changes of the apomyoglobin folding intermediate

2. How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway

3. Apomyoglobin stability as dependent on urea concentration and temperature at two pH values

4. Formation of a Molten Globule Intermediate Early in the Kinetic Folding Pathway of Apomyoglobin

5. Three-state protein folding: Experimental determination of free-energy profile

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