Folding of Protein G B1 Domain Studied by the Conformational Characterization of Fragments Comprising Its Secondary Structure Elements
- 1 June 1995
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 230 (2) , 634-649
- https://doi.org/10.1111/j.1432-1033.1995.0634h.x
Abstract
No abstract availableThis publication has 64 references indexed in Scilit:
- Trifluoroethanol-induced Stabilization of the α-Helical Structure of β-Lactoglobulin: Implication for Non-hierarchical Protein FoldingJournal of Molecular Biology, 1995
- Elucidating the Folding Problem of Helical Peptides using Empirical Parameters. III>Temperature and pH DependenceJournal of Molecular Biology, 1995
- Elucidating the Folding Problem of Helical Peptides using Empirical Parameters. II†. Helix Macrodipole Effects and Rational Modification of the Helical Content of Natural PeptidesJournal of Molecular Biology, 1995
- Helix Stop and Start Signals in Peptides and ProteinsJournal of Molecular Biology, 1994
- Local Conformations of Peptides Representing the Entire Sequence of Bovine Pancreatic Trypsin Inhibitor and Their Roles in FoldingJournal of Molecular Biology, 1993
- Folding of peptide fragments comprising the complete sequence of proteinsJournal of Molecular Biology, 1992
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- Characterization of low populated peptide helical structures in solution by means of NMR proton conformational shiftsBiochemical and Biophysical Research Communications, 1990
- A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromoleculesBiochemical and Biophysical Research Communications, 1980
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979