通过对Ile 3进行多次取代直接确定T4溶菌酶中的疏水稳定性。
Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3.
作者信息
Matsumura M, 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 Aug 4;334(6181):406-10. doi: 10.1038/334406a0.
DOI:10.1038/334406a0
PMID:3405287
Abstract
Replacing the isoleucine at amino-acid position three of bacteriophage T4 lysozyme causes changes in the thermodynamic stability of the protein that are directly related to the hydrophobicity of the substituted residue. Structural analysis confirms that the hydrophobic stabilization is proportional to the reduction of the surface area accessible to solvent on folding.
摘要
替换噬菌体T4溶菌酶氨基酸位置3处的异亮氨酸会导致该蛋白质热力学稳定性发生变化，这种变化与被取代残基的疏水性直接相关。结构分析证实，疏水稳定性与折叠时溶剂可及表面积的减少成正比。
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