Is folding of β-lactoglobulin non-hierarchic? intermediate with native-like β-sheet and non-native α-helix
- 3 March 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 296 (4) , 1039-1051
- https://doi.org/10.1006/jmbi.1999.3515
Abstract
No abstract availableKeywords
Funding Information
- Japan Society for the Promotion of Science
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 56 references indexed in Scilit:
- Is protein folding hierarchic? II. Folding intermediates and transition statesTrends in Biochemical Sciences, 1999
- Is protein folding hierarchic? I. Local structure and peptide foldingPublished by Elsevier ,1999
- Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteinsQuarterly Reviews of Biophysics, 1998
- Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopyJournal of Molecular Biology, 1998
- Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalinPublished by Elsevier ,1997
- Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesisNature, 1997
- Following protein folding in real time using NMR spectroscopyNature Structural & Molecular Biology, 1995
- Isotope effects in peptide group hydrogen exchangeProteins-Structure Function and Bioinformatics, 1993
- Primary structure effects on peptide group hydrogen exchangeProteins-Structure Function and Bioinformatics, 1993
- Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersionBiochemistry, 1972