通过与α-螺旋偶极相互作用的设计突变提高蛋白质热稳定性。
Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
作者信息
Nicholson H, Becktel W J, Matthews B W
机构信息
Institute of Molecular Biology, University of Oregon, Eugene 97403.
出版信息
Nature. 1988 Dec 15;336(6200):651-6. doi: 10.1038/336651a0.
DOI:10.1038/336651a0
PMID:3200317
Abstract
Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.
摘要
两种经过基因工程设计的氨基酸取代，旨在与T4溶菌酶中的α-螺旋偶极相互作用，结果表明它们能提高该蛋白质的热稳定性。对突变型溶菌酶结构的晶体学分析表明，这种稳定性的提高是由于静电相互作用，并不需要取代的氨基酸与α-螺旋末端之间有精确的氢键。
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