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- W2023604759 endingPage "e1002168" @default.
- W2023604759 startingPage "e1002168" @default.
- W2023604759 abstract "Allosteric regulation is a key component of cellular communication, but the way in which information is passed from one site to another within a folded protein is not often clear. While backbone motions have long been considered essential for long-range information conveyance, side-chain motions have rarely been considered. In this work, we demonstrate their potential utility using Monte Carlo sampling of side-chain torsional angles on a fixed backbone to quantify correlations amongst side-chain inter-rotameric motions. Results indicate that long-range correlations of side-chain fluctuations can arise independently from several different types of interactions: steric repulsions, implicit solvent interactions, or hydrogen bonding and salt-bridge interactions. These robust correlations persist across the entire protein (up to 60 Å in the case of calmodulin) and can propagate long-range changes in side-chain variability in response to single residue perturbations." @default.
- W2023604759 created "2016-06-24" @default.
- W2023604759 creator A5001938789 @default.
- W2023604759 creator A5019934984 @default.
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- W2023604759 date "2011-09-29" @default.
- W2023604759 modified "2023-10-05" @default.
- W2023604759 title "Long-Range Intra-Protein Communication Can Be Transmitted by Correlated Side-Chain Fluctuations Alone" @default.
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- W2023604759 doi "https://doi.org/10.1371/journal.pcbi.1002168" @default.
- W2023604759 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3182858" @default.
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