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PIC: Protein Interactions Calculator
Interactions within a protein structure and interactions between proteins in an assembly are essential considerations in understanding molecular basis of stability and functions of proteins and their complexes. There are several weak and strong interactions that render stability to a protein structu...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1933215/ https://www.ncbi.nlm.nih.gov/pubmed/17584791 http://dx.doi.org/10.1093/nar/gkm423 |
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author | Tina, K. G. Bhadra, R. Srinivasan, N. |
author_facet | Tina, K. G. Bhadra, R. Srinivasan, N. |
author_sort | Tina, K. G. |
collection | PubMed |
description | Interactions within a protein structure and interactions between proteins in an assembly are essential considerations in understanding molecular basis of stability and functions of proteins and their complexes. There are several weak and strong interactions that render stability to a protein structure or an assembly. Protein Interactions Calculator (PIC) is a server which, given the coordinate set of 3D structure of a protein or an assembly, computes various interactions such as disulphide bonds, interactions between hydrophobic residues, ionic interactions, hydrogen bonds, aromatic–aromatic interactions, aromatic–sulphur interactions and cation–π interactions within a protein or between proteins in a complex. Interactions are calculated on the basis of standard, published criteria. The identified interactions between residues can be visualized using a RasMol and Jmol interface. The advantage with PIC server is the easy availability of inter-residue interaction calculations in a single site. It also determines the accessible surface area and residue-depth, which is the distance of a residue from the surface of the protein. User can also recognize specific kind of interactions, such as apolar–apolar residue interactions or ionic interactions, that are formed between buried or exposed residues or near the surface or deep inside. |
format | Text |
id | pubmed-1933215 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-19332152007-07-31 PIC: Protein Interactions Calculator Tina, K. G. Bhadra, R. Srinivasan, N. Nucleic Acids Res Articles Interactions within a protein structure and interactions between proteins in an assembly are essential considerations in understanding molecular basis of stability and functions of proteins and their complexes. There are several weak and strong interactions that render stability to a protein structure or an assembly. Protein Interactions Calculator (PIC) is a server which, given the coordinate set of 3D structure of a protein or an assembly, computes various interactions such as disulphide bonds, interactions between hydrophobic residues, ionic interactions, hydrogen bonds, aromatic–aromatic interactions, aromatic–sulphur interactions and cation–π interactions within a protein or between proteins in a complex. Interactions are calculated on the basis of standard, published criteria. The identified interactions between residues can be visualized using a RasMol and Jmol interface. The advantage with PIC server is the easy availability of inter-residue interaction calculations in a single site. It also determines the accessible surface area and residue-depth, which is the distance of a residue from the surface of the protein. User can also recognize specific kind of interactions, such as apolar–apolar residue interactions or ionic interactions, that are formed between buried or exposed residues or near the surface or deep inside. Oxford University Press 2007-07 2007-06-21 /pmc/articles/PMC1933215/ /pubmed/17584791 http://dx.doi.org/10.1093/nar/gkm423 Text en © 2007 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Tina, K. G. Bhadra, R. Srinivasan, N. PIC: Protein Interactions Calculator |
title | PIC: Protein Interactions Calculator |
title_full | PIC: Protein Interactions Calculator |
title_fullStr | PIC: Protein Interactions Calculator |
title_full_unstemmed | PIC: Protein Interactions Calculator |
title_short | PIC: Protein Interactions Calculator |
title_sort | pic: protein interactions calculator |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1933215/ https://www.ncbi.nlm.nih.gov/pubmed/17584791 http://dx.doi.org/10.1093/nar/gkm423 |
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