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Oxford University Press, Nucleic Acids Research, W1(40), p. W348-W351, 2012

DOI: 10.1093/nar/gks447

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Protein frustratometer: a tool to localize energetic frustration in protein molecules

Journal article published in 2012 by Michael Jenik, R. Gonzalo Parra, R. Gonzalo Parra ORCID, Leandro G. Radusky, Adrian Turjanski, Peter G. Wolynes, Diego U. Ferreiro ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The frustratometer is an energy landscape theory-inspired algorithm that aims at quantifying the location of frustration manifested in protein molecules. Frustration is a useful concept for gaining insight to the proteins biological behavior by analyzing how the energy is distributed in protein structures and how mutations or conformational changes shift the energetics. Sites of high local frustration often indicate biologically important regions involved in binding or allostery. In contrast, minimally frustrated linkages comprise a stable folding core of the molecule that is conserved in conformational changes. Here, we describe the implementation of these ideas in a webserver freely available at the National EMBNet node—Argentina, at URL: http://lfp.qb.fcen.uba.ar/embnet/.