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Analysis of peptide rotational diffusion by homonuclear NMR
Author(s) -
Malliavin Thérèse E.,
Giudice Emmanuel
Publication year - 2002
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10128
Subject(s) - homonuclear molecule , chemistry , rotational diffusion , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , diffusion , nuclear overhauser effect , molecule , isotropy , conformational isomerism , analytical chemistry (journal) , stereochemistry , organic chemistry , thermodynamics , physics , quantum mechanics
The analysis of the rotational diffusion of a molecule using homonuclear NMR is investigated. The homonuclear longitudinal and transverse cross‐relaxation rates, which can be quantitatively measured using off‐Resonance Rotating frame nuclear Overhauser Effect Spectroscopy (ROESY), are used to build a distribution, which exhibits a solid‐state‐like pattern characteristic of the diffusion tensor. The distributions of the antimicrobial peptide ranalexin in water and in 30% of trifluoracetic acid (TFE) are compared, and the peptide rotational diffusion is shown to be more isotropic in water than in 30% TFE. This difference is further supported by the analysis of NMR ranalexin conformers in 30% TFE, and by the analysis of a molecular dynamics simulation of peptide in water. © 2002 Wiley Periodicals, Inc. Biopolymers 63: 335–342, 2002