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Elucidating Protein Binding Mechanisms by Variable‐ c ITC
Author(s) -
Freiburger Lee A.,
Auclair Karine,
Mittermaier Anthony K.
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200900614
Subject(s) - isothermal titration calorimetry , ambiguity , allosteric regulation , variable (mathematics) , set (abstract data type) , computer science , computational biology , chemistry , biochemistry , biology , mathematics , programming language , mathematical analysis , enzyme
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.