Backbone motion in elastin's hydrophobic domains as detected by (2) H NMR spectroscopy.
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.
Department of Chemistry, University of Hawaii, Honolulu, HI 96822, USA. kumashir@hawaii.edu
Kristin K
KK
Kumashiro
Kosuke
K
Ohgo
Douglas W
DW
Elliott
Todd F
TF
Kagawa
Walter P
WP
Niemczura
D000818:Animals; D000831:Animals, Newborn; D016880:Anisotropy; D003903:Deuterium; D004548:Elasticity; D004549:Elastin / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D005998:Glycine / Q000737:chemistry* / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D007553:Isotope Labeling; D009038:Motion; D032389:Myocytes, Smooth Muscle / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D051381:Rats; D013696:Temperature; D014867:Water
D014867:Water; D004549:Elastin; D003903:Deuterium; D005998:Glycine