Internal motional amplitudes and correlated bond rotations in an alpha-helical peptide derived from 13C and 15N NMR relaxation.

Peptide GFSKAELAKARAAKRGGY folds in an alpha-helical conformation that is stabilized by formation of a hydrophobic staple motif and an N-terminal capping box (Munoz V. Blanco FJ, Serrano L, 1995, Struct Biol 2:380-385). To investigate backbone and side-chain internal motions within the helix and hyd...

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Main Authors: Idiyatullin, D., Krushelnitsky, A., Nesmelova, I., Blanco, F., Daragan, V. A., Serrano, L., Mayo, K. H.
Format: Artigo
Jezik:Inglês
Izdano: Cold Spring Harbor Laboratory Press 2000
Teme:
Research Article
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144496/
https://ncbi.nlm.nih.gov/pubmed/11152123
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