This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at firstname.lastname@example.org
Backbone motion in elastin's hydrophobic domains as detected by 2H NMR spectroscopy†
Article first published online: 13 AUG 2012
Copyright © 2012 Wiley Periodicals, Inc.
Volume 97, Issue 11, pages 882–888, November 2012
How to Cite
Kumashiro, K. K., Ohgo, K., Elliott, D. W., Kagawa,, T. F. and Niemczura, W. P. (2012), Backbone motion in elastin's hydrophobic domains as detected by 2H NMR spectroscopy. Biopolymers, 97: 882–888. doi: 10.1002/bip.22094
- Issue published online: 13 AUG 2012
- Article first published online: 13 AUG 2012
- Accepted manuscript online: 17 MAY 2012 06:37AM EST
- Manuscript Accepted: 10 MAY 2012
- Manuscript Revised: 6 MAY 2012
- Manuscript Received: 7 OCT 2011
- National Science Foundation. Grant Number: MCB-0344975 and MCB-1022526
- solid-state NMR;
The elasticity of vertebrate tissue originates from the insoluble, cross-linked protein elastin. Here, the results of variable-temperature 2H 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.