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Title: | PROTEIN ALLOSTERY: FROM BASIC MECHANISMS TO COMPUTATIONAL MODELLING | Authors: | TEE WEI VEN | Keywords: | allostery, protein dynamics, computational modelling, mutation, intrinsic disorder | Issue Date: | 1-Jul-2020 | Citation: | TEE WEI VEN (2020-07-01). PROTEIN ALLOSTERY: FROM BASIC MECHANISMS TO COMPUTATIONAL MODELLING. ScholarBank@NUS Repository. | Abstract: | Allostery is a phenomenon in which a protein’s functional activity is regulated by a perturbation at a distant site. Allosteric control of proteins by ligand binding, mutations, and structural disorder is explored here using a structure-based statistical mechanical model of allostery. The following findings will be presented: first, reversing allosteric communication identifies known allosteric sites and suggests latent allosteric sites; second, Allosteric Signaling Maps (ASMs), derived by exhaustive mutational scanning over all amino acids, allow to examine the allosteric effects of distal mutations quantitatively; third, allosteric regulation driven by structural disorder and order, and their transitions, will be explored in several proteins. The computationally efficient method is implemented as an online web-server called AlloSigMA2 to quantify the allosteric signaling originated from user-defined site(s) and/or mutation(s). Lastly, an online database AlloMAPS which contains the comprehensive description on allosteric signaling in more than 2,000 proteins and protein domains will be presented. | URI: | https://scholarbank.nus.edu.sg/handle/10635/185740 |
Appears in Collections: | Ph.D Theses (Open) |
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