Self-Consistent Framework Connecting Experimental Proxies of Protein Dynamics with Configurational Entropy.

ABSTRACT: The recently developed NMR techniques enable estimation of protein configurational entropy change from the change in the average methyl order parameters. This experimental observable, however, does not directly measure the contribution of intramolecular couplings, protein main-chain motions, or angular dynamics. Here, we carry out a self-consistent computational analysis of the impact of these missing contributions on an extensive set of molecular dynamics simulations of different proteins undergoing binding. Specifically, we compare the configurational entropy change in protein complex formation as obtained by the maximum information spanning tree approximation (MIST), which treats the above entropy contributions directly, and the change in the average NMR methyl and NH order parameters.

SUBMITTER: Fleck M 

PROVIDER: S-EPMC9245193 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature