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- W2071623887 abstract "Large-scale flexibility within a multidomain protein often plays an important role in its biological function. Despite its inherent low resolution, small-angle x-ray scattering (SAXS) is well suited to investigate protein flexibility and determine, with the help of computational modeling, what kinds of protein conformations would coexist in solution. In this article, we develop a tool that combines SAXS data with a previously developed sampling technique called amplified collective motions (ACM) to elucidate structures of highly dynamic multidomain proteins in solution. We demonstrate the use of this tool in two proteins, bacteriophage T4 lysozyme and tandem WW domains of the formin-binding protein 21. The ACM simulations can sample the conformational space of proteins much more extensively than standard molecular dynamics (MD) simulations. Therefore, conformations generated by ACM are significantly better at reproducing the SAXS data than are those from MD simulations." @default.
- W2071623887 created "2016-06-24" @default.
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- W2071623887 date "2014-08-01" @default.
- W2071623887 modified "2023-10-02" @default.
- W2071623887 title "Characterization of Protein Flexibility Using Small-Angle X-Ray Scattering and Amplified Collective Motion Simulations" @default.
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- W2071623887 doi "https://doi.org/10.1016/j.bpj.2014.07.005" @default.
- W2071623887 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4142251" @default.
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