PMID: 9183535Jun 1, 1997Paper

The role of long-range interactions in defining the secondary structure of proteins is overestimated

Computer Applications in the Biosciences : CABIOS
A FiserI Simon

Abstract

Secondary structure predictions based on the properties of individual residues, and sometimes on local interactions, usually fail to exceed 65% efficiency. Therefore, non-local, long-range interactions seem to be a significant cause of this limitation. In this paper, we apply approaches to localize highly interacting residues and clusters of residues involved in multiple non-local interactions, and test various secondary structure predictions on this separate subset to assess the effect of long-range interactions on the prediction efficiencies. It was found that only a marginal part of the failure of secondary structure predictions results from the presence of long-range interactions. Alternative possibilities are also discussed.

Citations

Nov 3, 2001·Biochimica Et Biophysica Acta·I SimonG E Tusnády
Dec 19, 2007·Biochimie·Guilhem FaureAlexandre G de Brevern
Jul 1, 2005·Protein Science : a Publication of the Protein Society·Daisuke Kihara
Jul 17, 2009·IEEE Transactions on Neural Networks·Jinmiao Chen, Narendra S Chaudhari
Apr 28, 2004·Journal of Molecular Biology·Monika FuxreiterPeter Tompa
Aug 29, 2006·Journal of Molecular Biology·Amrita MohanVladimir N Uversky

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