Structural and dynamic characterization of an unfolded state of poplar apo‐plastocyanin formed under nondenaturing conditions
Open Access
- 1 May 2001
- journal article
- Published by Wiley in Protein Science
- Vol. 10 (5) , 1056-1066
- https://doi.org/10.1110/ps.00601
Abstract
Protein Science, the flagship journal of The Protein Society, serves an international forum for publishing original reports on all scientific aspects of protein molecules. The Journal publishes papers by leading scientists from all over the world that report on advances in the understanding of proteins in the broadest sense. Protein Science aims to unify this field by cutting across established disciplinary lines and focusing on “protein-centered” science.Keywords
This publication has 71 references indexed in Scilit:
- 1H, 13C and 15N chemical shift referencing in biomolecular NMRJournal of Biomolecular NMR, 1995
- Partially Folded Conformation of the (30-51) Intermediate in the Disulphide Folding Pathway of Bovine Pancreatic Trypsin Inhibitor: 1H and 15N Resonance Assignments and Determination of Backbone Dynamics from 15N Relaxation MeasurementsJournal of Molecular Biology, 1993
- Correlation of Backbone Amide and Aliphatic Side-Chain Resonances in 13C/15N-Enriched Proteins by Isotropic Mixing of 13C MagnetizationJournal of Magnetic Resonance, Series B, 1993
- An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteinsJournal of Magnetic Resonance (1969), 1992
- Folding of peptide fragments comprising the complete sequence of proteinsJournal of Molecular Biology, 1992
- Improved 3D triple-resonance NMR techniques applied to a 31 kDa proteinJournal of Magnetic Resonance (1969), 1992
- Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteinsJournal of Magnetic Resonance (1969), 1990
- Structure of oxidized poplar plastocyanin at 1·6 Å resolutionJournal of Molecular Biology, 1983
- Molecular dynamics and structure of the random coil and helical states of the collagen peptide, α1-CB2, as determined by 13C magnetic resonanceBiochemistry, 1975
- Conformational energy estimates for statistically coiling polypeptide chainsJournal of Molecular Biology, 1967