title: Resolving nitrogen-15 and proton chemical shifts for mobile segments of elastin with two-dimensional NMR spectroscopy.
abstract: In this study, one- and two-dimensional NMR experiments are applied to uniformly (15)N-enriched synthetic elastin, a recombinant human tropoelastin that has been cross-linked to form an elastic hydrogel. Hydrated elastin is characterized by large segments that undergo "liquid-like" motions that limit the efficiency of cross-polarization. The refocused insensitive nuclei enhanced by polarization transfer experiment is used to target these extensive, mobile regions of this protein. Numerous peaks are detected in the backbone amide region of the protein, and their chemical shifts indicate the completely unstructured, "random coil" model for elastin is unlikely. Instead, more evidence is gathered that supports a characteristic ensemble of conformations in this rubber-like protein.
authors.affiliation: Department of Chemistry, University of Hawaii, Honolulu, Hawaii 96822, USA.
authors.forename: Kosuke
authors.initials: K
authors.lastname: Ohgo
authors.forename: Walter P
authors.initials: WP
authors.lastname: Niemczura
authors.forename: Brian C
authors.initials: BC
authors.lastname: Seacat
authors.forename: Steven G
authors.initials: SG
authors.lastname: Wise
authors.forename: Anthony S
authors.initials: AS
authors.lastname: Weiss
authors.forename: Kristin K
authors.initials: KK
authors.lastname: Kumashiro
mesh_terms: D004549:Elastin / Q000737:chemistry*; D006801:Humans; D009587:Nitrogen Isotopes / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011522:Protons; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D009587:Nitrogen Isotopes; D011522:Protons; D011994:Recombinant Proteins; D004549:Elastin