Kinetic stability of membrane proteins

被引：20
作者：
González Flecha F.L. [1 ]
机构：
[1] Universidad de Buenos Aires, CONICET, Laboratorio de Biofísica Molecular, Instituto de Química y Fisicoquímica Biológicas, Buenos Aires
来源：
Biophysical Reviews | 2017年 / 9卷 / 5期
关键词：
Irreversible denaturation; Kinetic analysis; Membrane enzymes; P-ATPases; Protein unfolding; Thermal stability;
D O I：
10.1007/s12551-017-0324-0
中图分类号：
学科分类号：
摘要：
Although membrane proteins constitute an important class of biomolecules involved in key cellular processes, study of the thermodynamic and kinetic stability of their structures is far behind that of soluble proteins. It is known that many membrane proteins become unstable when removed by detergent extraction from the lipid environment. In addition, most of them undergo irreversible denaturation, even under mild experimental conditions. This process was found to be associated with partial unfolding of the polypeptide chain exposing hydrophobic regions to water, and it was proposed that the formation of kinetically trapped conformations could be involved. In this review, we will describe some of the efforts toward understanding the irreversible inactivation of membrane proteins. Furthermore, its modulation by phospholipids, ligands, and temperature will be herein discussed. © 2017, International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany.
引用
收藏
页码：563 / 572
页数：9
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