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Structural insights into the elastin mimetic (LGGVG) 6 using solid‐state 13 C NMR experiments and statistical analysis of the PDB
Author(s) -
Kumashiro Kristin K.,
Ohgo Kosuke,
Niemczura Walter P.,
Onizuka Allen K.,
Asakura Tetsuo
Publication year - 2008
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.20984
Subject(s) - elastin , protein data bank (rcsb pdb) , chemistry , magic angle spinning , solid state nuclear magnetic resonance , nuclear magnetic resonance spectroscopy , crystallography , protein data bank , two dimensional nuclear magnetic resonance spectroscopy , protein structure , biophysics , nuclear magnetic resonance , stereochemistry , biochemistry , medicine , physics , pathology , biology
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. Using a combination of a statistical analysis based on structures in the Brookhaven Protein Data Bank (PDB), 1D cross‐polarization magic‐angle‐spinning (CPMAS) NMR spectroscopy, and 2D off‐magic‐angle‐spinning (OMAS) spin‐diffusion experiments, it is determined that none of the residues are found in a singular regular, highly ordered structure. Instead, like the poly(VPGVG) elastin mimetics, there are multiple conformations and significant disorder. Furthermore, the conformational ensembles are not reflective of proteins generally, as in the PDB, suggesting that the structure distributions in elastin mimetics are unique to these peptides and are a salient feature of the functional model of the native protein. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 668–679, 2008. 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 biopolymers@wiley.com