Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their display
<p>Abstract</p> <p>Background</p> <p>Depending on chemical features residues have preferred locations – interior or exterior – in protein structures, which also determine how many other residues are found around them. The close packing of residues is the hallmark of pro...
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| Format: | Article |
| Language: | English |
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BMC
2009-04-01
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| Series: | BMC Bioinformatics |
| Online Access: | http://www.biomedcentral.com/1471-2105/10/103 |
| _version_ | 1818055028873625600 |
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| author | Ray Partha Bahadur Ranjit Pal Arumay Chakrabarti Pinak |
| author_facet | Ray Partha Bahadur Ranjit Pal Arumay Chakrabarti Pinak |
| author_sort | Ray Partha |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>Depending on chemical features residues have preferred locations – interior or exterior – in protein structures, which also determine how many other residues are found around them. The close packing of residues is the hallmark of protein interior and protein-protein interaction sites.</p> <p>Results</p> <p>The average values of accessible surface area (ASA) and partner number (PN, the number of other residues within a distance of 4.5 Å from any atom of a given residue) of different residues have been determined and a webserver, ContPlot has been designed to display these values (relative to the average values) along the protein sequence. This would be useful to visually identify residues that are densely packed, or those involved in protein-protein interactions. The skewness observed in the distribution of PNs is indicative of the hydrophobic or hydrophilic nature of the residue. The variation of ASA with PN can be analytically expressed in terms of a cubic equation. These equations (one for each residue) can be used to estimate the ASA of a polypeptide chain using the PNs of the individual residues in the structure.</p> <p>Conclusion</p> <p>The atom-based PNs (obtained by counting surrounding atoms) are highly correlated to the residue-based PN, indicating that the latter can adequately capture the atomic details of packing. The average values of ASA and PN associated with each residue should be useful in protein structure prediction or fold-recognition algorithm. ContPlot would provide a handy tool to assess the importance of a residue in the protein structure or interaction site.</p> |
| first_indexed | 2024-12-10T12:06:26Z |
| format | Article |
| id | doaj.art-f9265dbd12234deca261df3246784a11 |
| institution | Directory Open Access Journal |
| issn | 1471-2105 |
| language | English |
| last_indexed | 2024-12-10T12:06:26Z |
| publishDate | 2009-04-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Bioinformatics |
| spelling | doaj.art-f9265dbd12234deca261df3246784a112022-12-22T01:49:28ZengBMCBMC Bioinformatics1471-21052009-04-0110110310.1186/1471-2105-10-103Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their displayRay ParthaBahadur RanjitPal ArumayChakrabarti Pinak<p>Abstract</p> <p>Background</p> <p>Depending on chemical features residues have preferred locations – interior or exterior – in protein structures, which also determine how many other residues are found around them. The close packing of residues is the hallmark of protein interior and protein-protein interaction sites.</p> <p>Results</p> <p>The average values of accessible surface area (ASA) and partner number (PN, the number of other residues within a distance of 4.5 Å from any atom of a given residue) of different residues have been determined and a webserver, ContPlot has been designed to display these values (relative to the average values) along the protein sequence. This would be useful to visually identify residues that are densely packed, or those involved in protein-protein interactions. The skewness observed in the distribution of PNs is indicative of the hydrophobic or hydrophilic nature of the residue. The variation of ASA with PN can be analytically expressed in terms of a cubic equation. These equations (one for each residue) can be used to estimate the ASA of a polypeptide chain using the PNs of the individual residues in the structure.</p> <p>Conclusion</p> <p>The atom-based PNs (obtained by counting surrounding atoms) are highly correlated to the residue-based PN, indicating that the latter can adequately capture the atomic details of packing. The average values of ASA and PN associated with each residue should be useful in protein structure prediction or fold-recognition algorithm. ContPlot would provide a handy tool to assess the importance of a residue in the protein structure or interaction site.</p>http://www.biomedcentral.com/1471-2105/10/103 |
| spellingShingle | Ray Partha Bahadur Ranjit Pal Arumay Chakrabarti Pinak Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their display BMC Bioinformatics |
| title | Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their display |
| title_full | Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their display |
| title_fullStr | Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their display |
| title_full_unstemmed | Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their display |
| title_short | Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their display |
| title_sort | accessibility and partner number of protein residues their relationship and a webserver contplot for their display |
| url | http://www.biomedcentral.com/1471-2105/10/103 |
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