Work

Localizing frustration in native proteins and protein assemblies

Year: 2007

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.0709915104

Authors: Diego U. Ferreiro, Joseph A. Hegler, Elizabeth A. Komives, Peter G. Wolynes

Institutions: University of California San Diego, Center for Theoretical Biological Physics

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: G3701106356, IkB/NF-kB Recognition in Silico, In Vitro and In Vivo, Conceptual Aspects of Protein Folding