pH-induced structural transitions of caseins
- 1 June 2007
- journal article
- Published by Elsevier in Journal of Photochemistry and Photobiology B: Biology
- Vol. 87 (3) , 191-199
- https://doi.org/10.1016/j.jphotobiol.2007.04.004
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Amyloid Fibril Formation by Bovine Milk κ-Casein and Its Inhibition by the Molecular Chaperones αS- and β-CaseinBiochemistry, 2005
- 1,8-Anilinonaphthalene sulfonate binds to central cavity of human hemoglobinBiochemical and Biophysical Research Communications, 2004
- A biological perspective on the structure and function of caseins and casein micellesInternational Journal of Dairy Technology, 2004
- Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-SynucleinJournal of Biological Chemistry, 2001
- Evidence for a Partially Folded Intermediate in α-Synuclein Fibril FormationJournal of Biological Chemistry, 2001
- Conformational analysis of the hydrophobic peptide αs1-casein(136–196)Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
- Effect of self-association of αs1-casein and its cleavage fractions αs1-casein(136–196) and αs1-casein(1–197), on aromatic circular dichroic spectra: comparison with predicted modelsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
- Molecular Chaperone-like Properties of an Unfolded Protein, αs-CaseinJournal of Biological Chemistry, 1999
- Urea-Induced Unfolding and Conformational Stability of 3-Isopropylmalate Dehydrogenase from the Thermophile Thermus thermophilus and Its Mesophilic Counterpart from Escherichia coliBiochemistry, 1999
- Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probeBiopolymers, 1991