Tryptophan phosphorescence and pressure effects on protein structure

Patrizia Cioni, Giovanni B Strambini
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引用次数: 61

Abstract

After a brief introduction of the potentialities of Trp phosphorescence spectroscopy for probing the conformation and flexibility of protein structure, this presentation summarizes the effects of hydrostatic pressure (up to 3 kbar) on the native fold of monomeric and oligomeric proteins as inferred from the variation of the intrinsic phosphorescence lifetime and the oxygen and acrylamide bimolecular quenching rate constants of buried Trp residues. The pressure/temperature response of the globular fold and modulation of its dynamical structure is analyzed both in terms of a reduction of internal cavities and of hydration of the polypeptide. The implications of these findings for the thermodynamic stability of proteins and for the determination of subunit dissociation equilibria under high pressure conditions are also discussed.

色氨酸磷光和压力对蛋白质结构的影响
在简要介绍了色氨酸磷光光谱在探测蛋白质结构构象和柔韧性方面的潜力之后,本报告总结了静水压力(高达3 kbar)对单体和寡聚蛋白质天然折叠的影响,这是根据固有磷光寿命的变化以及埋藏色氨酸残基的氧和丙烯酰胺双分子猝灭速率常数推断的。从内部空腔的减少和多肽水合作用的角度分析了球状褶皱的压力/温度响应及其动态结构的调节。这些发现对蛋白质的热力学稳定性和在高压条件下测定亚基解离平衡的意义也进行了讨论。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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