13C NMR chemical shifts can predict disulfide bond formation
- 1 January 2000
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 18 (2) , 165-171
- https://doi.org/10.1023/a:1008398416292
Abstract
The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. In this study we demonstrate that 13C NMR chemical...Keywords
This publication has 7 references indexed in Scilit:
- Cα and Cβ Carbon-13 Chemical Shifts in Proteins From an Empirical DatabaseJournal of Biomolecular NMR, 1999
- 1H, 13C and 15N chemical shift referencing in biomolecular NMRJournal of Biomolecular NMR, 1995
- 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effectsJournal of Biomolecular NMR, 1995
- The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift dataJournal of Biomolecular NMR, 1994
- Disulfide bond isomerization in BPTI and BPTI(G36S): An NMR study of correlated mobility in proteinsBiochemistry, 1993
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- Conformations of disulfide bridges in proteinsInternational Journal of Peptide and Protein Research, 1990