Automatic Determination of Protein Backbone Resonance Assignments from Triple Resonance Nuclear Magnetic Resonance Data
- 1 January 2001
- book chapter
- Published by Elsevier
- Vol. 339, 91-108
- https://doi.org/10.1016/s0076-6879(01)39311-4
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- Linear prediction spectral analysis of NMR dataProgress in Nuclear Magnetic Resonance Spectroscopy, 1999
- TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large ProteinsJournal of the American Chemical Society, 1999
- High-resolution solution NMR structure of the Z domain of staphylococcal protein AJournal of Molecular Biology, 1997
- NMR Structural Analysis of an Analog of an Intermediate Formed in the Rate-Determining Step of One Pathway in the Oxidative Folding of Bovine Pancreatic Ribonuclease A: Automated Analysis of 1H, 13C, and 15N Resonance Assignments for Wild-Type and [C65S, C72S] Mutant FormsBiochemistry, 1997
- 1H, 13C and 15N chemical shift referencing in biomolecular NMRJournal of Biomolecular NMR, 1995
- An improved strategy for determining resonance assignments for isotopically enriched proteins and its application to an engineered domain of staphylococcal protein ABiochemistry, 1993
- Pulsed-field gradient-enhanced three-dimensional NMR experiment for correlating 13C.alpha./.beta., 13C', and 1H.alpha. chemical shifts in uniformly carbon-13-labeled proteins dissolved in waterJournal of the American Chemical Society, 1993
- A relational database for sequence-specific protein NMR dataJournal of Biomolecular NMR, 1991
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982