Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
Architectures and functional coverage of protein-protein interfaces
Download
index.pdf
Date
2008-09-05
Author
Tunçbağ, Nurcan
Guney, Emre
NUSSINOV, Ruth
Keskin, Ozlem
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
229
views
0
downloads
Cite This
The diverse range of cellular functions is performed by a limited number of protein folds existing in nature. One may similarly expect that cellular functional diversity would be covered by a limited number of protein-protein interface architectures. Here, we present 8205 interface clusters, each representing a unique interface architecture. This data set of protein-protein interfaces is analyzed and compared with older data sets. We observe that the number of both biological and crystal interfaces increases significantly compared to the number of Protein Data Bank entries. Furthermore, we find that the number of distinct interface architectures grows at a much faster rate than the number of folds and is yet to level off. We further analyze the growth trend of the functional coverage by constructing functional interaction networks from interfaces. The functional coverage is also found to steadily increase. Interestingly, we also observe that despite the diversity of interface architectures, some are more favorable and frequently used, and of particular interest, are the ones that are also preferred in single chains.
Subject Keywords
Protein interfaces
,
Protein interaction
,
Structure and function
,
Binding
,
Interface database
URI
https://hdl.handle.net/11511/31156
Journal
JOURNAL OF MOLECULAR BIOLOGY
DOI
https://doi.org/10.1016/j.jmb.2008.04.071
Collections
Graduate School of Informatics, Article
Suggestions
OpenMETU
Core
Prediction of protein subcellular localization based on primary sequence data
Özarar, Mert; Atalay, Mehmet Volkan; Department of Computer Engineering (2003)
Subcellular localization is crucial for determining the functions of proteins. A system called prediction of protein subcellular localization (P2SL) that predicts the subcellular localization of proteins in eukaryotic organisms based on the amino acid content of primary sequences using amino acid order is designed. The approach for prediction is to nd the most frequent motifs for each protein in a given class based on clustering via self organizing maps and then to use these most frequent motifs as features...
Predicting Protein-Protein Interactions from the Molecular to the Proteome Level
Keskin, Ozlem; Tunçbağ, Nurcan; Gursoy, Attila (2016-04-27)
Identification of protein protein interactions (PPIs) is at the center of molecular biology considering the unquestionable role of proteins in cells. Combinatorial interactions result in a repertoire of multiple functions; hence, knowledge of PPI and binding regions naturally serve to functional proteomics and drug discovery. Given experimental limitations to find all interactions in a proteome, computational prediction/modeling of protein interactions is a prerequisite to proceed on the way to complete int...
Distance-based Indexing of Residue Contacts for Protein Structure Retrieval and Alignment
Sacan, Ahmet; Toroslu, İsmail Hakkı; Ferhatosmanoglu, Hakan (2008-10-10)
New protein structures are continuously being determined with the hope of deriving insights into the function and mechanisms of proteins, and consequently, protein structure repositories are growing by leaps and bounds. However, we are still far from having the right methods for sensitive and effective use of the available structural data. The fact that current structural analysis tools are impractical for large-scale applications have given rise to several approaches that try to quickly identify candidate ...
Structural characterization of recombinant bovine Go alpha by spectroscopy and homology modeling
MEGA TİBER, PINAR; Orun, Oya; Nacar, Cevdet; Sezerman, Ugur Osman; Severcan, Feride; Severcan, Mete; Matagne, Andre; KAN, BEKİ (2011-01-01)
Go, a member of heterotrimeric guanine nucleotide-binding proteins, is the most abundant form of G protein in the central and peripheral nervous systems. Go alpha has a significant role in neuronal development and function but its signal transduction mechanism remains to be clarified.
Parallelization of functional flow to predict protein functions
Akkoyun, Emrah; Can, Tolga; Department of Medical Informatics (2011)
Protein-protein interaction networks provide important information about what the biological function of proteins whose roles are unknown might be in a cell. These interaction networks were analyzed by a variety of approaches by running them on a single computer and the roles of the proteins identified were used to predict the function of the proteins unidentified. The functional flow is an approach that takes the network connectivity, distance effect, topology of the network with local and global views int...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
N. Tunçbağ, E. Guney, R. NUSSINOV, and O. Keskin, “Architectures and functional coverage of protein-protein interfaces,”
JOURNAL OF MOLECULAR BIOLOGY
, pp. 785–802, 2008, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/31156.