为什么“天然未折叠”蛋白质在生理条件下是无结构的？

Why are "natively unfolded" proteins unstructured under physiologic conditions?

作者信息

Uversky V N, Gillespie J R, Fink A L

机构信息

Department of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, USA.

出版信息

Proteins. 2000 Nov 15;41(3):415-27. doi: 10.1002/1097-0134(20001115)41:3<415::aid-prot130>3.0.co;2-7.

DOI:10.1002/1097-0134(20001115)41:3<415::aid-prot130>3.0.co;2-7

PMID:11025552

Abstract

"Natively unfolded" proteins occupy a unique niche within the protein kingdom in that they lack ordered structure under conditions of neutral pH in vitro. Analysis of amino acid sequences, based on the normalized net charge and mean hydrophobicity, has been applied to two sets of proteins: small globular folded proteins and "natively unfolded" ones. The results show that "natively unfolded" proteins are specifically localized within a unique region of charge-hydrophobicity phase space and indicate that a combination of low overall hydrophobicity and large net charge represent a unique structural feature of "natively unfolded" proteins.

摘要

“天然未折叠”蛋白质在蛋白质王国中占据着独特的位置，因为它们在体外中性pH条件下缺乏有序结构。基于归一化净电荷和平均疏水性的氨基酸序列分析已应用于两组蛋白质：小的球状折叠蛋白质和“天然未折叠”蛋白质。结果表明，“天然未折叠”蛋白质特异性地定位在电荷-疏水性相空间的一个独特区域内，这表明低总体疏水性和大净电荷的组合代表了“天然未折叠”蛋白质的独特结构特征。