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PINT: Protein–protein Interactions Thermodynamic Database

The first release of Protein–protein Interactions Thermodynamic Database (PINT) contains >1500 data of several thermodynamic parameters along with sequence and structural information, experimental conditions and literature information. Each entry contains numerical data for the free energy change...

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Detalles Bibliográficos
Autores principales: Kumar, M. D. Shaji, Gromiha, M. Michael
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1347380/
https://www.ncbi.nlm.nih.gov/pubmed/16381844
http://dx.doi.org/10.1093/nar/gkj017
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author Kumar, M. D. Shaji
Gromiha, M. Michael
author_facet Kumar, M. D. Shaji
Gromiha, M. Michael
author_sort Kumar, M. D. Shaji
collection PubMed
description The first release of Protein–protein Interactions Thermodynamic Database (PINT) contains >1500 data of several thermodynamic parameters along with sequence and structural information, experimental conditions and literature information. Each entry contains numerical data for the free energy change, dissociation constant, association constant, enthalpy change, heat capacity change and so on of the interacting proteins upon binding, which are important for understanding the mechanism of protein–protein interactions. PINT also includes the name and source of the proteins involved in binding, their Protein Information Resource, SWISS-PROT and Protein Data Bank (PDB) codes, secondary structure and solvent accessibility of residues at mutant positions, measuring methods, experimental conditions, such as buffers, ions and additives, and literature information. A WWW interface facilitates users to search data based on various conditions, feasibility to select the terms for output and different sorting options. Further, PINT is cross-linked with other related databases, PIR, SWISS-PROT, PDB and NCBI PUBMED literature database. The database is freely available at
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spelling pubmed-13473802006-01-25 PINT: Protein–protein Interactions Thermodynamic Database Kumar, M. D. Shaji Gromiha, M. Michael Nucleic Acids Res Article The first release of Protein–protein Interactions Thermodynamic Database (PINT) contains >1500 data of several thermodynamic parameters along with sequence and structural information, experimental conditions and literature information. Each entry contains numerical data for the free energy change, dissociation constant, association constant, enthalpy change, heat capacity change and so on of the interacting proteins upon binding, which are important for understanding the mechanism of protein–protein interactions. PINT also includes the name and source of the proteins involved in binding, their Protein Information Resource, SWISS-PROT and Protein Data Bank (PDB) codes, secondary structure and solvent accessibility of residues at mutant positions, measuring methods, experimental conditions, such as buffers, ions and additives, and literature information. A WWW interface facilitates users to search data based on various conditions, feasibility to select the terms for output and different sorting options. Further, PINT is cross-linked with other related databases, PIR, SWISS-PROT, PDB and NCBI PUBMED literature database. The database is freely available at Oxford University Press 2006-01-01 2005-12-28 /pmc/articles/PMC1347380/ /pubmed/16381844 http://dx.doi.org/10.1093/nar/gkj017 Text en © The Author 2006. Published by Oxford University Press. All rights reserved
spellingShingle Article
Kumar, M. D. Shaji
Gromiha, M. Michael
PINT: Protein–protein Interactions Thermodynamic Database
title PINT: Protein–protein Interactions Thermodynamic Database
title_full PINT: Protein–protein Interactions Thermodynamic Database
title_fullStr PINT: Protein–protein Interactions Thermodynamic Database
title_full_unstemmed PINT: Protein–protein Interactions Thermodynamic Database
title_short PINT: Protein–protein Interactions Thermodynamic Database
title_sort pint: protein–protein interactions thermodynamic database
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1347380/
https://www.ncbi.nlm.nih.gov/pubmed/16381844
http://dx.doi.org/10.1093/nar/gkj017
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