用于评估球状蛋白质疏水核心稳定性的热力学和立体化学参数。
Thermodynamic and stereochemical parameters to evaluate stability of hydrophobic cores of globular proteins.
作者信息
Trikulenko A V
机构信息
Franko Lvov State University, Lvov, 290005, Ukraine.
出版信息
Biochemistry (Mosc). 1998 Nov;63(11):1290-3.
PMID:9864468
Abstract
This work presents a hydrophobicity scale of nonpolar amino acids calculated by the method of Tanford. The evaluation of stability of hydrophobic cores of globular proteins using this hydrophobicity scale is described. Stereochemical and thermodynamic parameters are presented that make it possible to choose replacements for side chains of nonpolar amino acid residues in the hydrophobic cores in order to increase their stability.
摘要
这项工作展示了通过坦福德方法计算得到的非极性氨基酸的疏水性标度。描述了使用该疏水性标度对球状蛋白质疏水核心稳定性的评估。还给出了立体化学和热力学参数，这些参数使得为增加疏水核心中非极性氨基酸残基侧链的稳定性而选择其替代物成为可能。
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