Distance-Based Configurational Entropy of Proteins from Molecular Dynamics Simulations.

ABSTRACT: Estimation of configurational entropy from molecular dynamics trajectories is a difficult task which is often performed using quasi-harmonic or histogram analysis. An entirely different approach, proposed recently, estimates local density distribution around each conformational sample by measuring the distance from its nearest neighbors. In this work we show this theoretically well grounded the method can be easily applied to estimate the entropy from conformational sampling. We consider a set of systems that are representative of important biomolecular processes. In particular: reference entropies for amino acids in unfolded proteins are obtained from a database of residues not participating in secondary structure elements;the conformational entropy of folding of β2-microglobulin is compu

SUBMITTER: Fogolari F 

PROVIDER: S-EPMC4503633 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature