Alternative Protein-Protein Interfaces Are Frequent Exceptions
نویسندگان
چکیده
منابع مشابه
Alternative Protein-Protein Interfaces Are Frequent Exceptions
The intricate molecular details of protein-protein interactions (PPIs) are crucial for function. Therefore, measuring the same interacting protein pair again, we expect the same result. This work measured the similarity in the molecular details of interaction for the same and for homologous protein pairs between different experiments. All scores analyzed suggested that different experiments oft...
متن کاملpredictions 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...
متن کاملAre protein-protein interfaces special regions on a protein's surface?
Protein-protein interactions (PPIs) are involved in many cellular processes. Experimentally obtained protein quaternary structures provide the location of protein-protein interfaces, the surface region of a given protein that interacts with another. These regions are termed half-interfaces (HIs). Canonical HIs cover roughly one third of a protein's surface and were found to have more hydrophobi...
متن کاملCharacterization 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...
متن کاملAre protein-protein interfaces more conserved in sequence than the rest of the protein surface?
Protein interfaces are thought to be distinguishable from the rest of the protein surface by their greater degree of residue conservation. We test the validity of this approach on an expanded set of 64 protein-protein interfaces using conservation scores derived from two multiple sequence alignment types, one of close homologs/orthologs and one of diverse homologs/paralogs. Overall, we find tha...
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ژورنال
عنوان ژورنال: PLoS Computational Biology
سال: 2012
ISSN: 1553-7358
DOI: 10.1371/journal.pcbi.1002623