title: Physical and molecular bases of protein thermal stability and cold adaptation.
abstract: The molecular bases of thermal and cold stability and adaptation, which allow proteins to remain folded and functional in the temperature ranges in which their host organisms live and grow, are still only partially elucidated. Indeed, both experimental and computational studies fail to yield a fully precise and global physical picture, essentially because all effects are context-dependent and thus quite intricate to unravel. We present a snapshot of the current state of knowledge of this highly complex and challenging issue, whose resolution would enable large-scale rational protein design.
authors.affiliation: Department of BioModeling, BioInformatics and BioProcesses, Université Libre de Bruxelles, CP 165/61, Roosevelt Ave. 50, 1050 Brussels, Belgium; Interuniversity Institute of Bioinformatics in Brussels, Université Libre de Bruxelles, CP 263, Triumph Bld, 1050 Brussels, Belgium.
authors.forename: Fabrizio
authors.initials: F
authors.lastname: Pucci
authors.affiliation: Department of BioModeling, BioInformatics and BioProcesses, Université Libre de Bruxelles, CP 165/61, Roosevelt Ave. 50, 1050 Brussels, Belgium; Interuniversity Institute of Bioinformatics in Brussels, Université Libre de Bruxelles, CP 263, Triumph Bld, 1050 Brussels, Belgium. Electronic address: mrooman@ulb.ac.be.
authors.forename: Marianne
authors.initials: M
authors.lastname: Rooman
mesh_terms: D000222:Adaptation, Physiological; D055592:Biophysical Phenomena; D003080:Cold Temperature; D006801:Humans; D008024:Ligands; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D008024:Ligands; D011506:Proteins