title: Optimal design of thermally stable proteins.
abstract: For many biotechnological purposes, it is desirable to redesign proteins to be more structurally and functionally stable at higher temperatures. For example, chemical reactions are intrinsically faster at higher temperatures, so using enzymes that are stable at higher temperatures would lead to more efficient industrial processes. We describe an innovative and computationally efficient method called Improved Configurational Entropy (ICE), which can be used to redesign a protein to be more thermally stable (i.e. stable at high temperatures). This can be accomplished by systematically modifying the amino acid sequence via local structural entropy (LSE) minimization. The minimization problem is modeled as a shortest path problem in an acyclic graph with nonnegative weights and is solved efficiently using Dijkstra's method.
authors: Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
authors: Ryan M
authors: RM
authors: Bannen
authors: Vanitha
authors: V
authors: Suresh
authors: George N
authors: GN
authors: Phillips
authors: Stephen J
authors: SJ
authors: Wright
authors: Julie C
authors: JC
authors: Mitchell
mesh_terms: D000465:Algorithms; D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D019277:Entropy; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D013696:Temperature
chemical_list: D011506:Proteins