Probing nascent structures in peptides using natural abundance <sup>13</sup>C NMR relaxation and reduced spectral density mapping
Carolyn M. Slupsky(University of California, Davis), Matthew P. Crump(University of Bristol), Leo Spyracopoulos(University of Alberta), Brian D. Sykes(University of Alberta), Valerie Booth(Memorial University of Newfoundland)
Cited by 7
Related Papers
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
|Journal of Biomolecular NMR|1995|1.6k
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
|Journal of Biomolecular NMR|1995|1k
Solution structure and basis for functional activity of stromal cell‐derived factor‐1; dissociation of CXCR4 activation from binding and inhibition of HIV‐1
|The EMBO Journal|1997|730
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide
|Biochemistry|1992|585
Structural proteomics of an archaeon.
|Nature Structural Biology|2000|291