Intermediate formation at lower urea concentration in ‘B’ isomer of human serum albumin: a case study using domain specific ligands
- 1 January 2004
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 314 (1) , 166-173
- https://doi.org/10.1016/j.bbrc.2003.12.069
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Anion-induced folding of Staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediatesJournal of Molecular Biology, 1998
- Structure of pressure-induced denatured state of human serum albumin: a comparison with the intermediate in urea-induced denaturationPublished by Elsevier ,1998
- Time-resolved biophysical methods in the study of protein foldingCurrent Opinion in Structural Biology, 1996
- Intermediate States in Protein FoldingJournal of Molecular Biology, 1996
- Insights into protein folding using physical techniques: studies of lysozyme and α -lactalbuminPhilosophical Transactions Of The Royal Society B-Biological Sciences, 1995
- Kinetic and equilibrium intermediates in protein foldingProtein Engineering, Design and Selection, 1994
- Fluorescence Techniques for Studying Protein StructurePublished by Wiley ,1991
- Drug-binding and other physicochemical properties of a large tryptic and a large peptic fragment of human serum albuminBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersionBiochemistry, 1972
- pK change of imidazole groups in bovine serum albumin due to the conformational change at neutral pHBiochemistry, 1971