title: Localizing frustration in native proteins and protein assemblies.
abstract: We propose a method of quantifying the degree of frustration manifested by spatially local interactions in protein biomolecules. This method of localization smoothly generalizes the global criterion for an energy landscape to be funneled to the native state, which is in keeping with the principle of minimal frustration. A survey of the structural database shows that natural proteins are multiply connected by a web of local interactions that are individually minimally frustrated. In contrast, highly frustrated interactions are found clustered on the surface, often near binding sites. These binding sites become less frustrated upon complex formation.
authors: Center for Theoretical Biological Physics and Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0365, USA.
authors: Diego U
authors: DU
authors: Ferreiro
authors: Joseph A
authors: JA
authors: Hegler
authors: Elizabeth A
authors: EA
authors: Komives
authors: Peter G
authors: PG
authors: Wolynes
mesh_terms: D019295:Computational Biology; D008956:Models, Chemical; D008958:Models, Molecular; D009154:Mutation; D011485:Protein Binding / Q000502:physiology; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D011506:Proteins; D014867:Water