13C CPMAS NMR studies of the elastin-like polypeptide (LGGVG)n
13C CPMAS NMR studies of the elastin-like polypeptide (LGGVG)n
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DOI：
10.1002/bip.10470
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发表时间：
2003-10-01
期刊：
影响因子：
2.9
通讯作者：
Tamburro, AM
中科院分区：
文献类型：
--
作者：
Kumashiro, KK;Kurano, TL;Tamburro, AM
不溶性弹性蛋白的结构-功能关系的阐明通常是用弹性蛋白样多肽来探讨的。通过这种方式，这种广泛的生物聚合物中不同区域的表征可以以“分段”的方式进行。我们的固体核磁共振实验表明，(LGGVG)(N)与弹性蛋白和一些弹性蛋白多肽具有相似的结构，为模拟多肽的应用提供了支持。此外，先前的核磁共振和CD研究表明，弹性蛋白样多肽(LGGVG)(N)在溶液中的结构除了未折叠区域外，最好的描述是具有I型和II型β转角的混合的“构象系综”。我们的数据表明，多肽在固体状态下并不采用单一构象，这进一步支持了涉及显著构象异质性的弹性蛋白模型。(C)2003年威利期刊公司。
The elucidation of structure-function relationships in insoluble elastin is often approached using elastin-like polypeptides. In this manner, the characterization of the different regions in this extensive biopolymer may be facilitated in a "piece-wise" manner. Our solid-state NMR experiments indicate that (LGGVG)(n) has structural similarities to elastin and some elastin peptides, providing support for the utility of the mimetic peptides. Furthermore, previous NMR and CD studies indicated that the structure of the elastin-like polypeptide (LGGVG)(n) in solution is best described as a "conformational ensemble" with a mixture of type I and II beta-turns, in addition to unfolded regions. Our data indicate that the peptide does not adopt a single conformation in the solid state, lending further support to models for elastin that involve significant conformational heterogeneity. (C) 2003 Wiley Periodicals, Inc.