title: Combining NMR and molecular dynamics studies for insights into the allostery of small GTPase-protein interactions.
abstract: 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.
authors: Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH, USA.
authors: Liqun
authors: L
authors: Zhang
authors: Sabine
authors: S
authors: Bouguet-Bonnet
authors: Matthias
authors: M
authors: Buck
mesh_terms: D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D056004:Molecular Dynamics Simulation; D020559:Monomeric GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D011506:Proteins; D020559:Monomeric GTP-Binding Proteins