A simple and efficient method for predicting protein-protein interaction sites

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A simple and efficient method for predicting protein-protein interaction sites.

Computational methods for predicting protein-protein interaction sites based on structural data are characterized by an accuracy between 70 and 80%. Some experimental studies indicate that only a fraction of the residues, forming clusters in the center of the interaction site, are energetically important for binding. In addition, the analysis of amino acid composition has shown that residues lo...

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Running Title: Protein-Protein Interaction Sites Predicting Protein-Protein Interaction Sites From Amino Acid Sequence

We describe an approach for computational prediction of protein-protein interaction sites using a support vector machine (SVM) classifier. Interface residues and other surface residues were extracted from 115 proteins derived from a set of 70 heterocomplexes in PDB. The SVM classifier was trained to predict whether or not a surface residue is located in the interface based on the identity of th...

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Optimal docking area: a new method for predicting protein-protein interaction sites.

Understanding energetics and mechanism of protein-protein association remains one of the biggest theoretical problems in structural biology. It is assumed that desolvation must play an essential role during the association process, and indeed protein-protein interfaces in obligate complexes have been found to be highly hydrophobic. However, the identification of protein interaction sites from s...

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A Method for Predicting Protein-Protein Interaction Types

Protein-protein interactions (PPIs) govern basic cellular processes through signal transduction and complex formation. The diversity of those processes gives rise to a remarkable diversity of interactions types, ranging from transient phosphorylation interactions to stable covalent bonding. Despite our increasing knowledge on PPIs in humans and other species, their types remain relatively unexp...

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Progress and challenges in predicting protein-protein interaction sites

The identification of protein-protein interaction sites is an essential intermediate step for mutant design and the prediction of protein networks. In recent years a significant number of methods have been developed to predict these interface residues and here we review the current status of the field. Progress in this area requires a clear view of the methodology applied, the data sets used fo...

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ژورنال

عنوان ژورنال: Genetics and Molecular Research

سال: 2008

ISSN: 1676-5680

DOI: 10.4238/vol7-3x-meeting07