Combined use of 13C chemical shift and 1H??13C? heteronuclear NOE data in monitoring a protein NMR structure refinement
- 1 February 1995
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 5 (2) , 161-172
- https://doi.org/10.1007/bf00208807
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Overcoming Solvent Saturation-Transfer Artifacts in Protein NMR at Neutral pH. Application of Pulsed Field Gradients in Measurements of 1H-15N Overhauser EffectsJournal of Magnetic Resonance, Series B, 1994
- Structure of Human Des(1-45) Factor Xa at 2·2 Å ResolutionJournal of Molecular Biology, 1993
- Normal mode analysis of mouse epidermal growth factor: Characterization of the harmonic motionProteins-Structure Function and Bioinformatics, 1993
- Prospects for NMR of large proteinsJournal of Biomolecular NMR, 1993
- Critical functional requirement for the guanidinium group of the arginine 41 side chain of human epidermal growth factor as revealed by mutagenic inactivation and chemical reactivation.Journal of Biological Chemistry, 1992
- The solution structure of human transforming growth factor αEuropean Journal of Biochemistry, 1991
- Conformational characterization of a single-site mutant of murine epidermal growth factor (EGF) by 1H NMR provides evidence that leucine-47 is involved in the interactions with the EGF receptor.Proceedings of the National Academy of Sciences, 1989
- Prediction of the folding of short polypeptide segments by uniform conformational samplingBiopolymers, 1987
- Identification of two anti-parallel beta-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance.Proceedings of the National Academy of Sciences, 1986
- Toward the complete assignment of the carbon nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitorBiochemistry, 1986