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- W2336171845 endingPage "4740" @default.
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- W2336171845 abstract "Significance How exactly protein motions facilitate substrate recognition and catalysis has remained largely unanswered. Characterization of protein dynamics at atomistic level is essential to understanding function. Molecular dynamics and NMR are helpful in this regard; however, analyzing multidimensional data from very long molecular dynamics (MD) simulations to elucidate key dynamical features observed in NMR remains very challenging. We present results from an approach for data analysis in which dynamics is defined in terms of interresidue contact formation and breaking. Analyzing simulation data on a therapeutically important Cyclophilin A and carrying out NMR experiments, we uncovered remarkable and unprecedented changes in its motions at a site over 15 Å from the active site upon substrate binding and how mutation in this distal site affects catalysis." @default.
- W2336171845 created "2016-06-24" @default.
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- W2336171845 date "2016-04-11" @default.
- W2336171845 modified "2023-10-12" @default.
- W2336171845 title "Dynamical network of residue–residue contacts reveals coupled allosteric effects in recognition, catalysis, and mutation" @default.
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- W2336171845 doi "https://doi.org/10.1073/pnas.1523573113" @default.
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