Origins of globular structure in proteins

FEBS Letters

Doi, Nobuhide¹  Yanagawa, Hiroshi¹ 

[1] Mitsubishi Kasei Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194, Japan

关键词: Exon shuffling;    Membrane-bound enzyme;    Molecular chaperone;    Molten globule state;    Protein evolution;    Protein folding;    AP;    alkaline phosphatase;    ORF;    open reading frame;    TM;    transmembrane;   

DOI  :  10.1016/S0014-5793(98)00674-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Since natural proteins are the products of a long evolutionary process, the structural properties of present-day proteins should depend not only on physico-chemical constraints, but also on evolutionary constraints. Here we propose a model for protein evolution, in which membranes play a key role as a scaffold for supporting the gradual evolution from flexible polypeptides to well-folded proteins. We suggest that the folding process of present-day globular proteins is a relic of this putative evolutionary process. To test the hypothesis that membranes once acted as a cradle for the folding of globular proteins, extensive research on membrane proteins and the interactions of globular proteins with membranes will be required.

【 授权许可】

Unknown