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. Through the use of a combination of a statistical analysis based on the Protein Data Bank, one-dimensional cross-polarization magic-angle-spinning NMR spectroscopy, and two-dimensional off-magic-angle-spinning spin-diffusion experiments, it is determined that this tandem repeat does not form a regular, highly ordered structure. Instead, like the poly(VPGVG) elastin mimetics, the valine has a twofold heterogeneity, although the conformations of these two populations differ from one peptide to the other.
Ohgo
Kosuke
K
Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan.
Niemczura
Walter P
WP
Ashida
Jun
J
Okonogi
Michi
M
Asakura
Tetsuo
T
Kumashiro
Kristin K
KK
D000595:Amino Acid Sequence; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004549:Elastin / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D014633:Valine / Q000737:chemistry*
D010446:Peptide Fragments; D004549:Elastin; D014633:Valine