High throughput methods of assessing protein stability and aggregation

被引：96

作者：

Senisterra, Guillermo A. ^{[1
]}

Finerty, Patrick J., Jr. ^{[1
]}

机构：

[1] Struct Genom Consortium, Toronto, ON M5G 1L7, Canada

来源：

MOLECULAR BIOSYSTEMS | 2009年 / 5卷 / 03期

基金：

英国惠康基金;

关键词：

THERMAL SHIFT ASSAYS; ISOTHERMAL DENATURATION; CRYSTALLIZATION; LIGANDS; OPTIMIZATION;

D O I：

10.1039/b814377c

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The significant increase in the demand for purified protein for crystallization and structural studies has made necessary the development of multi-sample methods for identifying solution conditions that affect protein stability and aggregation. Conditions that stabilize proteins can improve protein puri. cation and crystallization. These methods can be used to identify small molecule compounds or inhibitors that interact with the purified proteins, and might serve as starting points for drug discovery. In this article three methods for measuring protein stability and aggregation are described and discussed: differential scanning fluorimetry (DSF), differential static light scattering (DSLS), and isothermal denaturation (ITD).

引用

页码：217 / 223

页数：7

共 40 条

[1] Microscale fluorescent thermal stability assay for membrane proteins [J].

Alexandrov, Alexander I. ;

Mileni, Mauro ;

Chien, Ellen Y. T. ;

Hanson, Michael A. ;

Stevens, Raymond C. .

STRUCTURE, 2008, 16 (03) :351-359

[2] Structural and chemical profiling of the human cytosolic sulfotransferases [J].

Allali-Hassani, Abdellah ;

Pan, Patricia W. ;

Dombrovski, Ludmila ;

Najmanovich, Rafael ;

Tempel, Wolfram ;

Dong, Aiping ;

Loppnau, Peter ;

Martin, Fernando ;

Thonton, Janet ;

Edwards, Aled M. ;

Bochkarev, Alexey ;

Plotnikov, Alexander N. ;

Vedadi, Masoud ;

Arrowsmith, Cheryl H. .

PLOS BIOLOGY, 2007, 5 (05) :1063-1078

[3]

ARAI K, 1981, J BIOL CHEM, V256, P5247

[4] STUDY OF STRONG TO ULTRATIGHT PROTEIN INTERACTIONS USING DIFFERENTIAL SCANNING CALORIMETRY [J].

BRANDTS, JF ;

LIN, LN .

BIOCHEMISTRY, 1990, 29 (29) :6927-6940

[5] Decrypting the biochemical function of an essential gene from Streptococcus pneumoniae using ThermoFluor® technology [J].

Carver, TE ;

Bordeau, B ;

Cummings, MD ;

Petrella, EC ;

Pucci, MJ ;

Zawadzke, LE ;

Dougherty, BA ;

Tredup, JA ;

Bryson, JW ;

Yanchunas, J ;

Doyle, ML ;

Witmer, MR ;

Nelen, MI ;

DesJarlais, RL ;

Jaeger, EP ;

Devine, H ;

Asel, ED ;

Springer, BA ;

Bone, R ;

Salemme, FR ;

Todd, MJ .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (12) :11704-11712

[6]

Christendat D, 2000, NAT STRUCT BIOL, V7, P903

[7]

Dobrovetsky Elena, 2005, Journal of Structural and Functional Genomics, V6, P33, DOI 10.1007/s10969-005-1363-5

[8] High-level production and optimization of monodispersity of 11β-hydroxysteroid dehydrogenase type 1 [J].

Elleby, B ;

Svensson, S ;

Wu, XQ ;

Stefansson, K ;

Nilsson, J ;

Hallén, D ;

Oppermann, U ;

Abrahmsén, L .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2004, 1700 (02) :199-207

[9] Thermofluor-based high-throughput stability optimization of proteins for structural studies [J].

Ericsson, Ulrika B. ;

Hallberg, B. Martin ;

DeTitta, George T. ;

Dekker, Niek ;

Nordlund, Par .

ANALYTICAL BIOCHEMISTRY, 2006, 357 (02) :289-298

[10] A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases [J].

Fedorov, Oleg ;

Marsden, Brian ;

Pogacic, Vanda ;

Rellos, Peter ;

Mueller, Susanne ;

Bullock, Alex N. ;

Schwaller, Juerg ;

Sundstrom, Michael ;

Knapp, Stefan .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (51) :20523-20528

← 1 2 3 4 →