Investigating by CD the molecular mechanism of elasticity of elastomeric proteins
Investigating by CD the molecular mechanism of elasticity of elastomeric proteins
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DOI：
10.1002/chir.20541
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发表时间：
2008-10-01
期刊：
影响因子：
2
通讯作者：
Tamburro, Antonio M.
中科院分区：
文献类型：
--
作者：
Bochicchio, Brigida;Pepe, Antonietta;Tamburro, Antonio M.
弹性蛋白广泛存在于动物界，其主要功能是赋予器官和组织弹性和恢复力。除了共同的功能特性外，弹性蛋白还具有共同的序列设计。它们通常由具有高含量甘氨酸残基的重复序列构成。从构象的角度来看，所有的弹性蛋白质，因为现在分析显示之间的动态平衡折叠（主要是β-转角）和扩展（聚脯氨酸II和β-链）的构象，可能是在起源的高熵的放松状态。事实上，弹性蛋白、lamprin、abductin以及肌联蛋白的PEVK结构域共享相同的构象系综，从而指向作为弹性起源的共同分子机制。CD光谱法代表了整体使用的适当光谱技术，因为其对PPII结构的存在特别敏感。它在弹性蛋白，外展蛋白，和lamprin以及最近分析的蛋白弹性蛋白的分子研究中的用途将被提出。
Elastomeric proteins are widespread in the animal kingdom, and their main function is to confer elasticity and resilience to organs and tissues. Besides common functional properties, elastomeric proteins share a common sequence design. They are usually constituted by repetitive sequences with a high content of glycine residues. From a conformational point of view, all the elastomeric proteins since now analyzed show a dynamic equilibria between folded (mainly beta-turns) and extended (polyproline II and beta-strands) conformations that could be at the origin of the high entropy of the relaxed state. As a matter of fact, elastin, lamprin, abductin, as well as the PEVK domain of titin share the same conformational ensemble, thus pointing to a common molecular mechanism as the origin of elasticity. CD spectroscopy represents the proper spectroscopic technique to be used overall because of its particular sensitivity to the presence of PPII structure. Its use in the molecular studies of elastin, abductin, and lamprin as well as the recently analyzed protein resilin will be presented.