通过傅里叶变换红外光谱法研究从头设计的蛋白质（α-l-α）₂中α-螺旋结构的压力稳定性。

Pressure stability of the alpha-helix structure in a de novo designed protein (alpha-l-alpha)(2) studied by FTIR spectroscopy.

作者信息

Takekiyo Takahiro, Takeda Naohiro, Isogai Yasuhiro, Kato Minoru, Taniguchi Yoshihiro

机构信息

Department of Applied Chemistry, Ritsumeikan University 1-1-1, Noji-higashi, Kusatsu, Shiga 525-8577, Japan.

出版信息

Biopolymers. 2007 Feb 5;85(2):185-8. doi: 10.1002/bip.20628.

DOI:10.1002/bip.20628

PMID:17103420

Abstract

The pressure-induced structural changes of a de novo designed four-helix bundle protein, (alpha-l-alpha)(2), in aqueous solution have been investigated by FTIR spectroscopy. Changes in the amide I' band intensity show that pressure induces disruption of tertiary interactions and stabilizes the solvated alpha-helical form. This may suggest that the exposure of the hydrophobic core to the solvent by pressure is not a sufficient condition for pressure-induced unfolding of the alpha-helices of proteins.

摘要

通过傅里叶变换红外光谱（FTIR）研究了一种全新设计的四螺旋束蛋白（α-l-α）2在水溶液中压力诱导的结构变化。酰胺I'带强度的变化表明，压力会导致三级相互作用的破坏，并使溶剂化的α-螺旋形式更加稳定。这可能表明，压力使疏水核心暴露于溶剂并非蛋白质α-螺旋压力诱导解折叠的充分条件。