Literature DB >> 9183535

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

A Fiser1, Z Dosztányi, I Simon.   

Abstract

MOTIVATION: 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.
RESULTS: 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.

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Year:  1997        PMID: 9183535     DOI: 10.1093/bioinformatics/13.3.297

Source DB:  PubMed          Journal:  Comput Appl Biosci        ISSN: 0266-7061


  2 in total

1.  The effect of long-range interactions on the secondary structure formation of proteins.

Authors:  Daisuke Kihara
Journal:  Protein Sci       Date:  2005-06-29       Impact factor: 6.725

2.  A word of caution about biological inference - Revisiting cysteine covalent state predictions.

Authors:  Eva Tüdős; Bálint Mészáros; András Fiser; István Simon
Journal:  FEBS Open Bio       Date:  2014-03-12       Impact factor: 2.693

  2 in total

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