title: ENCoM server: exploring protein conformational space and the effect of mutations on protein function and stability.
abstract: ENCoM is a coarse-grained normal mode analysis method recently introduced that unlike previous such methods is unique in that it accounts for the nature of amino acids. The inclusion of this layer of information was shown to improve conformational space sampling and apply for the first time a coarse-grained normal mode analysis method to predict the effect of single point mutations on protein dynamics and thermostability resulting from vibrational entropy changes. Here we present a web server that allows non-technical users to have access to ENCoM calculations to predict the effect of mutations on thermostability and dynamics as well as to generate geometrically realistic conformational ensembles. The server is accessible at: http://bcb.med.usherbrooke.ca/encom.
authors.affiliation: Department of Biochemistry, Faculty of Medicine and Health Sciences, University of Sherbrooke, Sherbrooke, Quebec, J1H 5N4, Canada.
authors.forename: Vincent
authors.initials: V
authors.lastname: Frappier
authors.affiliation: Department of Biochemistry, Faculty of Medicine and Health Sciences, University of Sherbrooke, Sherbrooke, Quebec, J1H 5N4, Canada.
authors.forename: Matthieu
authors.initials: M
authors.lastname: Chartier
authors.affiliation: Department of Biochemistry, Faculty of Medicine and Health Sciences, University of Sherbrooke, Sherbrooke, Quebec, J1H 5N4, Canada rafael.najmanovich@usherbrooke.ca.
authors.forename: Rafael J
authors.initials: RJ
authors.lastname: Najmanovich
mesh_terms: D019277:Entropy; D020407:Internet; D008958:Models, Molecular; D017354:Point Mutation; D011487:Protein Conformation; D055550:Protein Stability; D012984:Software; D013696:Temperature; D014732:Vibration