Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin
- 14 May 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 288 (4) , 673-688
- https://doi.org/10.1006/jmbi.1999.2687
Abstract
No abstract availableKeywords
Funding Information
- Engineering and Physical Sciences Research Council
- Biotechnology and Biological Sciences Research Council
- Medical Research Council
- European Commission
- Howard Hughes Medical Institute
- Wellcome Trust
This publication has 55 references indexed in Scilit:
- Mechanistic Studies of the Folding of Human Lysozyme and the Origin of Amyloidogenic Behavior in Its Disease-Related VariantsBiochemistry, 1999
- Detection of residue contacts in a protein folding intermediateProceedings of the National Academy of Sciences, 1997
- Protein Folding Monitored at Individual Residues During a Two-Dimensional NMR ExperimentScience, 1996
- Rapid formation of a molten globule intermediate in refolding of α-lactalbuminFolding and Design, 1996
- Following protein folding in real time using NMR spectroscopyNature Structural & Molecular Biology, 1995
- Primary structure effects on peptide group hydrogen exchangeProteins-Structure Function and Bioinformatics, 1993
- Structure and dynamics of the acid-denatured molten globule state of .alpha.-lactalbumin: a two-dimensional NMR studyBiochemistry, 1993
- 1H‐NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of α‐lactalbuminEuropean Journal of Biochemistry, 1992
- Crystal structure of human α-lactalbumin at 1·7 Å resolutionJournal of Molecular Biology, 1991
- Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbuminBiochemistry, 1989