Simple screening method for improving membrane protein thermostability

被引：34
|
作者：
Mancusso, Romina [1 ,2 ]
Karpowich, Nathan K. [1 ]
Czyzewski, Bryan K. [1 ,2 ]
Wang, Da-Neng [1 ]
机构：
[1] NYU, Sch Med, Helen L & Martin S Kimmel Ctr Biol & Med, Skirball Inst Biomol Med,Dept Cell Biol, New York, NY 10016 USA
[2] NYU, Sch Med, Struct Biol Grad Program, New York, NY 10016 USA
来源：
METHODS | 2011年 / 55卷 / 04期
基金：
美国国家卫生研究院;
关键词：
Membrane proteins; Size exclusion chromatography; Protein thermostability; UNDECAPRENYL PYROPHOSPHATE PHOSPHATASE; COLI GLYCEROL-3-PHOSPHATE TRANSPORTER; HUMAN ERYTHROCYTE-MEMBRANE; X-RAY-STRUCTURE; ESCHERICHIA-COLI; STRUCTURAL BASIS; HIGH-RESOLUTION; RHODOBACTER-SPHAEROIDES; FORMATE TRANSPORTER; THERMAL-STABILITY;
D O I：
10.1016/j.ymeth.2011.07.008
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Biochemical and biophysical analysis on integral membrane proteins often requires monodisperse and stable protein samples. Here we describe a method to characterize protein thermostability by measuring its melting temperature in detergent using analytical size-exclusion chromatography. This quantitative method can be used to screen for compounds and conditions that stabilize the protein. With this technique we were able to assess and improve the thermostability of several membrane proteins. These conditions were in turn used to assist purification, to identify protein ligand and to improve crystal quality. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码：324 / 329
页数：6
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