Conformations of peptide fragments from the FK506 binding protein: comparison with the native and urea-unfolded states
- 5 February 1999
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 285 (5) , 2161-2175
- https://doi.org/10.1006/jmbi.1998.2440
Abstract
No abstract availableKeywords
This publication has 94 references indexed in Scilit:
- Extracting Information from the Temperature Gradients of Polypeptide NH Chemical Shifts. 1. The Importance of Conformational AveragingJournal of the American Chemical Society, 1997
- Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the α-helix fragmentFolding and Design, 1997
- Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solutionFolding and Design, 1996
- A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein FoldingJournal of Molecular Biology, 1995
- The nature of protein folding pathways: The classical versus the new viewJournal of Biomolecular NMR, 1995
- Transferred Nuclear Overhauser Effect Study of the C-Terminal Helix of Yeast Phosphoglycerate Kinase: NMR Solution Structure of the C-Terminal Bound PeptideBiochemistry, 1995
- NMR Solution Structure of the Isolated N-Terminal Fragment of Protein-G B1 Domain. Evidence of Trifluoroethanol Induced Native-Like .beta.-Hairpin FormationBiochemistry, 1994
- Detection of local structures in reduced unfolded bovine pancreatic trypsin inhibitorProteins-Structure Function and Bioinformatics, 1992
- Reduced bovine pancreatic trypsin inhibitor has a compact structureBiochemistry, 1988
- Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frameJournal of the American Chemical Society, 1984