Kinetic studies of protein folding using NMR spectroscopy
- 1 July 1998
- journal article
- review article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 5 (7) , 504-507
- https://doi.org/10.1038/744
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Protein Folding: A Perspective from Theory and ExperimentAngewandte Chemie International Edition in English, 1998
- Refolding of [6-19F]Tryptophan-Labeled Escherichia coli Dihydrofolate Reductase in the Presence of Ligand: A Stopped-Flow NMR Spectroscopy StudyBiochemistry, 1998
- Time-resolved biophysical methods in the study of protein foldingCurrent Opinion in Structural Biology, 1996
- The concept of a random coil: Residual structure in peptides and denatured proteinsFolding and Design, 1996
- Direct NMR Measurement of the Folding Kinetics of a Trimeric PeptideBiochemistry, 1996
- Real-Time Refolding Studies of 6-19F-Tryptophan Labeled Escherichia coli Dihydrofolate Reductase Using Stopped-Flow NMR SpectroscopyBiochemistry, 1996
- NMR and protein folding: Equilibrium and stopped‐flow studiesProtein Science, 1993
- Pulsed H/D-exchange studies of folding intermediatesCurrent Opinion in Structural Biology, 1993
- Design of stopped-flow NMR rapid-mixing cellsReview of Scientific Instruments, 1975
- Stopped-flow nuclear magnetic resonance spectroscopyJournal of the American Chemical Society, 1972