Protein thermostability calculations using alchemical free energy simulations.

ABSTRACT: Thermal stability of proteins is crucial for both biotechnological and therapeutic applications. Rational protein engineering therefore frequently aims at increasing thermal stability by introducing stabilizing mutations. The accurate prediction of the thermodynamic consequences caused by mutations, however, is highly challenging as thermal stability changes are caused by alterations in the free energy of folding. Growing computational power, however, increasingly allows us to use alchemical free energy simulations, such as free energy perturbation or thermodynamic integration, to calculate free energy differences with relatively high accuracy. In this article, we present an automated protocol for setting up alchemical free energy calculations for mutations of naturally occurring amino aci

SUBMITTER: Seeliger D 

PROVIDER: S-EPMC2872215 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature