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• W2011035648 abstract "Ion charge pairs and hydrogen bonds have been extensively studied for their roles in stabilizing protein complexes and in steering the process of protein association. Recently, it has become clear that some protein complexes are dynamic in that they interconvert between several alternate configurations. We have previously characterized one such system: the EphA2:SHIP2 SAM-SAM heterodimer by solution NMR. Here we carried out extensive all-atom molecular-dynamics simulations on a microsecond time-scale starting with different NMR-derived structures for the complex. Transitions are observed between several discernible configurations at average time intervals of 50-100 ns. The domains reorient relative to one another by substantial rotation and a slight shifting of the interfaces. Bifurcated and intermediary salt-bridge and hydrogen-bond interactions play a role in the transitions in a process that can be described as moving along a monkey-bar. We notice an increased density of salt bridges near protein interaction surfaces that appear to enable these transitions, also suggesting why the trajectories can become kinetically hindered in regions where fewer of such interactions are possible. In this context, even microsecond molecular-dynamics simulations are not sufficient to sample the energy landscape unless the structures remain close to their experimentally derived low-energy configurations." @default.
• W2011035648 created "2016-06-24" @default.
• W2011035648 creator A5087321296 @default.
• W2011035648 creator A5087559484 @default.
• W2011035648 date "2013-11-01" @default.
• W2011035648 modified "2023-10-12" @default.
• W2011035648 title "Molecular Simulations of a Dynamic Protein Complex: Role of Salt-Bridges and Polar Interactions in Configurational Transitions" @default.
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• W2011035648 doi "https://doi.org/10.1016/j.bpj.2013.09.052" @default.
• W2011035648 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3838735" @default.
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• W2011035648 hasPublicationYear "2013" @default.
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