期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2003
卷号：100
期号：25
页码：14828-14833
DOI：10.1073/pnas.2432867100
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Conformational flexibility is important for protein function. However, information on the range of conformations accessible to macromolecules in the unbound state is often difficult to obtain. By using the model system of the tandem Src homology 2 domain (i.e., two adjacent Src homology 2 domains) of the Syk kinase, we report a method combining calorimetric and crystallographic measurements that reveals the preexistence of a conformational equilibrium in the unbound state, and that shows that this equilibrium is crucial for function.
