Internal motional amplitudes and correlated bond rotations in an alpha-helical peptide derived from 13C and 15N NMR relaxation.
Idiyatullin D, Krushelnitsky A, Nesmelova I, Blanco F, Daragan VA, Serrano L, Mayo KH.
Idiyatullin D, et al. Among authors: daragan va.
Protein Sci. 2000 Nov;9(11):2118-27. doi: 10.1110/ps.9.11.2118.
Protein Sci. 2000.
PMID: 11152123
Free PMC article.
For the side chain of hydrophobic staple residue F2, wobbling-in-a-cone type motions dominate in water, whereas in TFE, the Cbeta-Cgamma bond and phenyl ring fluctuate more simply about the Calpha-Cbeta bond. These data support the Daragan-Mayo model of correlated bond rot …
For the side chain of hydrophobic staple residue F2, wobbling-in-a-cone type motions dominate in water, whereas in TFE, the Cbeta-Cgamma bon …