Hierarchical unfolding of the α-lactalbumin molten globule: presence of a compact intermediate without a unique tertiary fold
- 1 April 2000
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 298 (1) , 1-6
- https://doi.org/10.1006/jmbi.2000.3660
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Role of the molten globule state in protein foldingAdvances in Protein Chemistry, 2000
- Defining the core structure of the α-lactalbumin molten globule stateJournal of Molecular Biology, 1999
- Is protein folding hierarchic? II. Folding intermediates and transition statesTrends in Biochemical Sciences, 1999
- Effect of the Extra N-terminal Methionine Residue on the Stability and Folding of Recombinant α-Lactalbumin Expressed in Escherichia coliJournal of Molecular Biology, 1999
- Is protein folding hierarchic? I. Local structure and peptide foldingPublished by Elsevier ,1999
- Peptide models of local and long-range interactions in the molten globule state of human α-lactalbuminJournal of Molecular Biology, 1998
- Rapid formation of a molten globule intermediate in refolding of α-lactalbuminFolding and Design, 1996
- Crystal structure of human α-lactalbumin at 1·7 Å resolutionJournal of Molecular Biology, 1991
- Origins of structure in globular proteins.Proceedings of the National Academy of Sciences, 1990
- Theory for the folding and stability of globular proteinsBiochemistry, 1985