Mechanistic investigation of domain specific unfolding of human serum albumin and the effect of sucrose-Reference-Cited by-同舟云学术

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Mechanistic investigation of domain specific unfolding of human serum albumin and the effect of sucrose

Published:2013-09-18 Issue:11 Volume:22 Page:1571-1581
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Yadav Rajeev¹,Sen Pratik¹

Affiliation:

1. Department of Chemistry; Indian Institute of Technology Kanpur; Kanpur 208 016 Uttar Pradesh India

Funder

Fellowship to RY, University Grant Commission, Government of India

Board of Research in Nuclear Sciences (BRNS), Department of Atomic Energy (DAE), Government of India

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2357/fullpdf

Reference74 articles.

1. Unfolding free energy changes determined by the linear extrapolation method. Unfolding of phenylmethanesulphonyl α-chymotrypsin using different denaturants;Santoro;Biochemistry,1988

2. Equilibrium constants and free energies in unfolding of proteins in urea solutions;Klotz;Proc Natl Acad Sci USA,1996

3. Comparative studies of unfolding and binding of ligands to human serum albumin in the presence of fatty acid: spectroscopic approach;Varshney;Int J Biol Macromol,2008

4. Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation;Muzammil;Proteins,2000

5. Chemically induced unfolding of bovine serum albumin by urea and sodium dodecyl sulfate: a spectral study with the polarity-sensitive charge-transfer fluorescent probe (E)−3-(4-methylaminophenyl) acrylic acid methyl ester;Ghosh;ChemPhysChem,2009

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