DOCKGROUND resource for studying protein-protein interfaces

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DOCKGROUND resource for studying protein-protein interfaces

MOTIVATION Public resources for studying protein interfaces are necessary for better understanding of molecular recognition and developing intermolecular potentials, search procedures and scoring functions for the prediction of protein complexes. RESULTS The first release of the DOCKGROUND resource implements a comprehensive database of co-crystallized (bound-bound) protein-protein complexes,...

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DOCKGROUND protein-protein docking decoy set

UNLABELLED A protein-protein docking decoy set is built for the Dockground unbound benchmark set. The GRAMM-X docking scan was used to generate 100 non-native and at least one near-native match per complex for 61 complexes. The set is a publicly available resource for the development of scoring functions and knowledge-based potentials for protein docking methodologies. AVAILABILITY The decoys...

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predictions of protein-protein interfaces within membrane protein complexes

background: prediction of interaction sites within the membrane protein complexes using the sequence data is of a great importance, because it would find applications in modification of molecules transport through membrane, signaling pathways and drug targets of many diseases. nevertheless, it has gained little attention from the protein structural bioinformatics community. methods: in this stu...

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Characterization of protein-protein interfaces.

We analyze the characteristics of protein-protein interfaces using the largest datasets available from the Protein Data Bank (PDB). We start with a comparison of interfaces with protein cores and non-interface surfaces. The results show that interfaces differ from protein cores and non-interface surfaces in residue composition, sequence entropy, and secondary structure. Since interfaces, protei...

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Protein domain interfaces: characterization and comparison with oligomeric protein interfaces.

The physical and chemical properties of domain-domain interactions have been analysed in two-domain proteins selected from the protein classification, CATH. The two-domain structures were divided into those derived from (i) monomeric proteins, or (ii) oligomeric or complexed proteins. The size, polarity, hydrogen bonding and packing of the intra-chain domain interface were calculated for both s...

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ژورنال

عنوان ژورنال: Bioinformatics

سال: 2006

ISSN: 1367-4803,1460-2059

DOI: 10.1093/bioinformatics/btl447