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National Academy of Sciences, Proceedings of the National Academy of Sciences, 50(104), p. 19819-19824, 2007

DOI: 10.1073/pnas.0709915104

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Localizing frustration in native proteins and protein assemblies

Journal article published in 2007 by Diego U. Ferreiro ORCID, Joseph A. Hegler, Elizabeth A. Komives, Peter G. Wolynes
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.