Folding of a β-sheet Protein Monitored by Real-time NMR Spectroscopy
- 16 May 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 328 (5) , 1161-1171
- https://doi.org/10.1016/s0022-2836(03)00349-8
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Structural and dynamic characterization of an unfolded state of poplar apo‐plastocyanin formed under nondenaturing conditionsProtein Science, 2001
- Cooperativity of a Protein Folding Reaction Probed at Multiple Chain Positions by Real-Time 2D NMR SpectroscopyBiochemistry, 2000
- Kinetic studies of protein folding using NMR spectroscopyNature Structural & Molecular Biology, 1998
- Protein Folding Monitored at Individual Residues During a Two-Dimensional NMR ExperimentScience, 1996
- Following protein folding in real time using NMR spectroscopyNature Structural & Molecular Biology, 1995
- Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerizationBiochemistry, 1993
- Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbuminBiochemistry, 1989
- NMR evidence for an early framework intermediate on the folding pathway of ribonuclease ANature, 1988
- The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide.Journal of Biological Chemistry, 1984
- Structure of oxidized poplar plastocyanin at 1·6 Å resolutionJournal of Molecular Biology, 1983