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SBION: A Program for Analyses of Salt-Bridges from Multiple Structure Files
Salt-bridge and network salt-bridge are specific electrostatic interactions that contribute to the overall stability of proteins. In hierarchical protein folding model, these interactions play crucial role in nucleation process. The advent and growth of protein structure database and its availabilit...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Biomedical Informatics
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3974244/ https://www.ncbi.nlm.nih.gov/pubmed/24748757 http://dx.doi.org/10.6026/97320630010164 |
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author | Gupta, Parth Sarthi Sen Mondal, Sudipta Mondal, Buddhadev Islam, Rifat Nawaz Ul Banerjee, Shyamashree Bandyopadhyay, Amal K |
author_facet | Gupta, Parth Sarthi Sen Mondal, Sudipta Mondal, Buddhadev Islam, Rifat Nawaz Ul Banerjee, Shyamashree Bandyopadhyay, Amal K |
author_sort | Gupta, Parth Sarthi Sen |
collection | PubMed |
description | Salt-bridge and network salt-bridge are specific electrostatic interactions that contribute to the overall stability of proteins. In hierarchical protein folding model, these interactions play crucial role in nucleation process. The advent and growth of protein structure database and its availability in public domain made an urgent need for context dependent rapid analysis of salt-bridges. While these analyses on single protein is cumbersome and time-consuming, batch analyses need efficient software for rapid topological scan of a large number of protein for extracting details on (i) fraction of salt-bridge residues (acidic and basic). (ii) Chain specific intra-molecular salt-bridges, (iii) inter-molecular salt-bridges (protein-protein interactions) in all possible binary combinations (iv) network salt-bridges and (v) secondary structure distribution of salt-bridge residues. To the best of our knowledge, such efficient software is not available in public domain. At this juncture, we have developed a program i.e. SBION which can perform all the above mentioned computations for any number of protein with any number of chain at any given distance of ion-pair. It is highly efficient, fast, error-free and user friendly. Finally we would say that our SBION indeed possesses potential for applications in the field of structural and comparative bioinformatics studies. AVAILABILITY: SBION is freely available for non-commercial/academic institutions on formal request to the corresponding author (akbanerjee@biotech.buruniv.ac.in). |
format | Online Article Text |
id | pubmed-3974244 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
spelling | pubmed-39742442014-04-18 SBION: A Program for Analyses of Salt-Bridges from Multiple Structure Files Gupta, Parth Sarthi Sen Mondal, Sudipta Mondal, Buddhadev Islam, Rifat Nawaz Ul Banerjee, Shyamashree Bandyopadhyay, Amal K Bioinformation Software Salt-bridge and network salt-bridge are specific electrostatic interactions that contribute to the overall stability of proteins. In hierarchical protein folding model, these interactions play crucial role in nucleation process. The advent and growth of protein structure database and its availability in public domain made an urgent need for context dependent rapid analysis of salt-bridges. While these analyses on single protein is cumbersome and time-consuming, batch analyses need efficient software for rapid topological scan of a large number of protein for extracting details on (i) fraction of salt-bridge residues (acidic and basic). (ii) Chain specific intra-molecular salt-bridges, (iii) inter-molecular salt-bridges (protein-protein interactions) in all possible binary combinations (iv) network salt-bridges and (v) secondary structure distribution of salt-bridge residues. To the best of our knowledge, such efficient software is not available in public domain. At this juncture, we have developed a program i.e. SBION which can perform all the above mentioned computations for any number of protein with any number of chain at any given distance of ion-pair. It is highly efficient, fast, error-free and user friendly. Finally we would say that our SBION indeed possesses potential for applications in the field of structural and comparative bioinformatics studies. AVAILABILITY: SBION is freely available for non-commercial/academic institutions on formal request to the corresponding author (akbanerjee@biotech.buruniv.ac.in). Biomedical Informatics 2014-03-19 /pmc/articles/PMC3974244/ /pubmed/24748757 http://dx.doi.org/10.6026/97320630010164 Text en © 2014 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited. |
spellingShingle | Software Gupta, Parth Sarthi Sen Mondal, Sudipta Mondal, Buddhadev Islam, Rifat Nawaz Ul Banerjee, Shyamashree Bandyopadhyay, Amal K SBION: A Program for Analyses of Salt-Bridges from Multiple Structure Files |
title | SBION: A Program for Analyses of Salt-Bridges from Multiple Structure Files |
title_full | SBION: A Program for Analyses of Salt-Bridges from Multiple Structure Files |
title_fullStr | SBION: A Program for Analyses of Salt-Bridges from Multiple Structure Files |
title_full_unstemmed | SBION: A Program for Analyses of Salt-Bridges from Multiple Structure Files |
title_short | SBION: A Program for Analyses of Salt-Bridges from Multiple Structure Files |
title_sort | sbion: a program for analyses of salt-bridges from multiple structure files |
topic | Software |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3974244/ https://www.ncbi.nlm.nih.gov/pubmed/24748757 http://dx.doi.org/10.6026/97320630010164 |
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