Elucidating Protein Binding Mechanisms by Variable-c ITC

被引：48

作者：

Freiburger, Lee A. ^{[1
]}

Auclair, Karine ^{[1
]}

Mittermaier, Anthony K. ^{[1
]}

机构：

[1] McGill Univ, Dept Chem, Montreal, PQ H3A 2K6, Canada

来源：

CHEMBIOCHEM | 2009年 / 10卷 / 18期

基金：

加拿大自然科学与工程研究理事会; 加拿大健康研究院;

关键词：

aminoglycoside acetyltransferase; biological interactions; calorimetry; cooperative effects; isothermal titration calorimetry; ISOTHERMAL TITRATION CALORIMETRY; ENTEROCOCCUS-FAECIUM; COOPERATIVITY; CONSTANTS;

D O I：

10.1002/cbic.200900614

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：

Isothermal titration calorimetry (ITC) has great potential for studying allosteric and cooperative interactions. However, a single set of ITC data can be compatible with several different binding models; this leaves the actual binding mechanism uncertain. Here we report a simple approach for resolving this ambiguity, based on a global analysis of variable-c value ITC datasets obtained with a range of sample concentrations. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：2871 / 2873

页数：3

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