Characterization and analysis of binding of Thioflavin T with partially folded and native states of α–lactalbumin protein by calorimetric and spectroscopic techniques
Authors:
- 1 February 2017
- journal article
- Published by Elsevier in International Journal of Biological Macromolecules
- Vol. 95, 376-384
Abstract
No abstract availableKeywords
Funding Information
- Indian Institute of Technology Bombay
This publication has 40 references indexed in Scilit:
- The how’s and why’s of protein folding intermediatesArchives of Biochemistry and Biophysics, 2013
- Interactions of thioflavin T with serum albumins: Spectroscopic analysesSpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 2009
- Mechanism of thioflavin T binding to amyloid fibrilsJournal of Structural Biology, 2005
- Specific Compositions of Amyloid-β Peptides as the Determinant of Toxic β-AggregationJournal of Biological Chemistry, 2003
- α‐Lactalbumin: structure and functionFEBS Letters, 2000
- Is the molten globule a third phase of proteins?Proceedings of the National Academy of Sciences, 1998
- The molten globule state of α‐lactalbuminThe FASEB Journal, 1996
- Structure and dynamics of the acid-denatured molten globule state of .alpha.-lactalbumin: a two-dimensional NMR studyBiochemistry, 1993
- The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structureProteins: Structure, Function, and Bioinformatics, 1989
- Protein folding: Hypotheses and experimentsThe Protein Journal, 1987