title: Energetic profiling of protein folds.
abstract: Current protein classification methods treat high-resolution structures as static entities. However, experiments have well documented the dynamic nature of proteins. With knowledge that thermodynamic fluctuations around the high-resolution structure contribute to a more physically accurate and biologically meaningful picture of a protein, the concept of a protein's energetic profile is introduced. It is demonstrated on a large scale that energetic profiles are both diagnostic of a protein fold and evolutionarily relevant. Development of Structural Thermodynamic Ensemble-based Protein Homology (STEPH), an algorithm that searches for local similarities between energetic profiles, constitutes a first step towards a long-term goal of our laboratory to integrate thermodynamic information into protein-fold classification approaches.
authors.affiliation: Department of Biochemistry and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas, USA.
authors.forename: Jason
authors.initials: J
authors.lastname: Vertrees
authors.forename: James O
authors.initials: JO
authors.lastname: Wrabl
authors.forename: Vincent J
authors.initials: VJ
authors.lastname: Hilser
mesh_terms: D000465:Algorithms; D000818:Animals; D006801:Humans; D008954:Models, Biological; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D011506:Proteins