Benjamin J. Killian

TL;DR: A method is presented for extracting the configurational entropy of solute molecules from molecular dynamics simulations, in which the entropy is computed as an expansion of multidimensional mutual information terms, which account for correlated motions among the various internal degrees of freedom of the molecule.

TL;DR: The results indicate that the truncation of the MIE at the two‐body level can be an accurate, computationally nondemanding approximation to the configurational entropy of anharmonic internal degrees of freedom.

TL;DR: In this paper, the authors applied the mutual information expansion (MIE) method to protein-ligand binding using multiple molecular dynamics simulations to study the association of the ubiquitin E2 variant domain of the protein Tsg101 and an HIV-derived nonapeptide.

TL;DR: This work applies information-theoretic expansions of the configurational entropy to well-sampled molecular dynamics simulations of a model host–guest system and the protein bovine pancreatic trypsin inhibitor to indicate that changes in correlation are important determinants of entropy changes for biologically relevant processes and thatChanges in correlation may either balance or reinforce changes in first-order entropy.

TL;DR: It is suggested that low-order correlations suffice to describe most of the conformational fluctuations of molecules in a thermal environment.