Altered dynamics upon oligomerization corresponds to key functional sites.

ABSTRACT: It is known that over half of the proteins encoded by most organisms function as oligomeric complexes. Oligomerization confers structural stability and dynamics changes in proteins. We investigate the effects of oligomerization on protein dynamics and its functional significance for a set of 145 multimeric proteins. Using coarse-grained elastic network models, we inspect the changes in residue fluctuations upon oligomerization and then compare with residue conservation scores to identify the functional significance of these changes. Our study reveals conservation of about ½ of the fluctuations, with ¼ of the residues increasing in their mobilities and ¼ having reduced fluctuations. The residues with dampened fluctuations are evolutionarily more conserved and can serve as orthosteric bindin

SUBMITTER: Mishra SK 

PROVIDER: S-EPMC6953176 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature