Heterogeneity in the Conformation of Valine in the Elastin Mimetic (LGGVG)6 as Shown by Solid-State 13C NMR Spectroscopy

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• 作者：Kosuke Ohgo ; Walter P. Niemczura ; Jun Ashida ; Michi Okonogi ; Tetsuo Asakura ; Kristin K. Kumashiro
• 刊名：Biomacromolecules
• 出版年：2006
• 出版时间：December 2006
• 年：2006
• 卷：7
• 期：12
• 页码：3306 - 3310
• 全文大小：262K
• 年卷期：v.7,no.12(December 2006)
• ISSN：1526-4602

文摘

Elastin is an abundant protein found in vertebrates and is the source of elasticity in connective tissues and bloodvessels. The repeating polypeptide sequences found in the hydrophobic domains of elastin have been the focusof many studies that attempt to understand the function of the native protein on a molecular scale. In thiscommunication, the (LGGVG)₆ elastin mimetic is characterized by solid-state ¹³C NMR spectroscopy. Throughthe use of a combination of a statistical analysis based on the Protein Data Bank, one-dimensional cross-polarizationmagic-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 thepoly(VPGVG) elastin mimetics, the valine has a twofold heterogeneity, although the conformations of these twopopulations differ from one peptide to the other.