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Backbone motion in elastin's hydrophobic domains as detected by 2 H NMR spectroscopy
Author(s) -
Kumashiro Kristin K.,
Ohgo Kosuke,
Elliott Douglas W.,
Kagawa, Todd F.,
Niemczura Walter P.
Publication year - 2012
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.22094
Subject(s) - chemistry , elastin , isotropy , nuclear magnetic resonance spectroscopy , crystallography , spectroscopy , spectral line , anisotropy , nmr spectra database , nuclear magnetic resonance , stereochemistry , medicine , physics , pathology , quantum mechanics , astronomy
Abstract The elasticity of vertebrate tissue originates from the insoluble, cross‐linked protein elastin. Here, the results of variable‐temperature 2 H NMR spectra are reported for hydrated elastin that has been enriched at the Hα position in its abundant glycines. Typical powder patterns reflecting averaged quadrupolar parameters are observed for the frozen protein, as opposed to the two, inequivalent deuterons that are detected in a powder sample of enriched glycine. The spectra of the hydrated elastin at warmer temperatures are dominated by a strong central peak with features close to the baseline, reflective of both isotropic and very weakly anisotropic motions. © 2012 Wiley Periodicals, Inc. Biopolymers 97:882–888, 2012.