Combining NMR and molecular dynamics studies for insights into the allostery of small GTPase-protein interactions.
Combining NMR and molecular dynamics studies for insights into the allostery of small GTPase-protein interactions.
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DOI：
10.1007/978-1-61779-334-9_13
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Buck, Matthias
中科院分区：
文献类型：
--
作者：
Zhang, Liqun;Bouguet-Bonnet, Sabine;Buck, Matthias
Combinations of experimentally derived data from nuclear magnetic resonance spectroscopy and analyses of molecular dynamics trajectories increasingly allow us to obtain a detailed description of the molecular mechanisms by which proteins function in signal transduction. This chapter provides an introduction into these two methodologies, illustrated by example of a small GTPase–effector interaction. It is increasingly becoming clear that new insights are provided by the combination of experimental and computational methods. Understanding the structural and protein dynamical contributions to allostery will be useful for the engineering of new binding interfaces and protein functions, as well as for the design/in silico screening of chemical agents that can manipulate the function of small GTPase–protein interactions in diseases such as cancer.
