Acrylamide Quenching of apo- and holo-α-Lactalbumin in Guanidine Hydrochloride
Authors:
- Steven H. GrossmanSGSteven H. Grossman
- 1 March 2000
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 269 (3) , 709-712
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- The molten globule state of α‐lactalbuminThe FASEB Journal, 1996
- A Protein Dissection Study of a Molten GlobuleBiochemistry, 1994
- Intrinsic tryptophan fluorescence of Schizosaccharomyces pombe mitochondrial F1-ATPase. A powerful probe for phosphate and nucleotide interactionsBiochemistry, 1991
- The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structureProteins: Structure, Function, and Bioinformatics, 1989
- Environment of tryptophan residues in various conformational states of α-lactalbumin studied by time-resolved and steady-state fluorescence spectroscBiophysical Chemistry, 1988
- Ca2+ Alteration in the Unfolding Behavior of α-Lactalbumin1The Journal of Biochemistry, 1986
- Cation binding effects on the pH, thermal and urea denaturation transitions in α-lactalbuminBiophysical Chemistry, 1985
- Fluorescence quenching studies with proteinsAnalytical Biochemistry, 1981
- Comparative fluorescence properties of bovine, goat, human and guinea pig α lactalbuminBiophysical Chemistry, 1980
- Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studiesBiochemistry, 1976