Unfoldness of the denatured state of proteins determines urea: Methylamine counteraction in terms of Gibbs free energy of stabilization-Reference-Cited by-同舟云学术

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Unfoldness of the denatured state of proteins determines urea: Methylamine counteraction in terms of Gibbs free energy of stabilization

Published:2019-07 Issue: Volume:132 Page:666-676
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Rahman Safikur,Islam Asimul,Hassan Md. Imtaiyaz,Kim Jihoe,Ahmad Faizan

Funder

National Centre for Biological Sciences

Tata Institute of Fundamental Research

Department of Science and Technology

Science and Engineering Research Board

Indian National Science Academy

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference48 articles.

1. The salt relations of marine and halophilic species of the unicellular green alga,Dunaliella

2. Living with Water Stress: Evolution of Osmolyte Systems

3. Influence of molecular and chemical chaperones on protein folding

4. Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses

5. Testing the Ability of Non-Methylamine Osmolytes Present in Kidney Cells to Counteract the Deleterious Effects of Urea on Structure, Stability and Function of Proteins

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