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.

Resolving nitrogen-15 and proton chemical shifts for mobile segments of elastin with two-dimensional NMR spectroscopy.

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.

De-Pake-ing transform analysis of fully deuterated malonic acid.

The analysis of deuterium wideline NMR spectra has been an essential step in characterizing the dynamics of molecules in the solid-state. Although clearly important, the identification of quadrupolar coupling constants (QCCs) from the powder patterns is often complicated by poor sensitivity and/or spectral overlap. Previously, others have demonstrated the utility of "de-Pake-ing", a mathematical transform that yields the QCCs in a straightforward manner for symmetric (eta=0) sites.

Structural insights into the elastin mimetic (LGGVG)6 using solid-state 13C NMR experiments and statistical analysis of the PDB.

Elastin is a crosslinked hydrophobic protein found in abundance in vertebrate tissue and is the source of elasticity in connective tissues and blood vessels. The repeating polypeptide sequences found in the hydrophobic domains of elastin have been the focus of many studies that attempt to understand the function of the native protein on a molecular scale. In this study, the central residues of the (LGGVG)(6) elastin mimetic are targeted.

Heterogeneity in the conformation of valine in the elastin mimetic (LGGVG)6 as shown by solid-state 13C NMR SPEctroscopy.

Elastin is an abundant protein found in vertebrates and is the source of elasticity in connective tissues and blood vessels. The repeating polypeptide sequences found in the hydrophobic domains of elastin have been the focus of many studies that attempt to understand the function of the native protein on a molecular scale. In this communication, the (LGGVG)6 elastin mimetic is characterized by solid-state 13C NMR spectroscopy.