Cavities and atomic packing in protein structures and interfaces.
A comparative analysis of cavities enclosed in a tertiary structure of proteins and interfaces formed by the interaction of two protein subunits in obligate and non-obligate categories (represented by homodimeric molecules and heterocomplexes, respectively) is presented. The total volume of cavities...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2008-09-01
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| Series: | PLoS Computational Biology |
| Online Access: | http://europepmc.org/articles/PMC2582456?pdf=render |
| _version_ | 1819009665127677952 |
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| author | Shrihari Sonavane Pinak Chakrabarti |
| author_facet | Shrihari Sonavane Pinak Chakrabarti |
| author_sort | Shrihari Sonavane |
| collection | DOAJ |
| description | A comparative analysis of cavities enclosed in a tertiary structure of proteins and interfaces formed by the interaction of two protein subunits in obligate and non-obligate categories (represented by homodimeric molecules and heterocomplexes, respectively) is presented. The total volume of cavities increases with the size of the protein (or the interface), though the exact relationship may vary in different cases. Likewise, for individual cavities also there is quantitative dependence of the volume on the number of atoms (or residues) lining the cavity. The larger cavities tend to be less spherical, solvated, and the interfaces are enriched in these. On average 15 A(3) of cavity volume is found to accommodate single water, with another 40-45 A(3) needed for each additional solvent molecule. Polar atoms/residues have a higher propensity to line solvated cavities. Relative to the frequency of occurrence in the whole structure (or interface), residues in beta-strands are found more often lining the cavities, and those in turn and loop the least. Any depression in one chain not complemented by a protrusion in the other results in a cavity in the protein-protein interface. Through the use of the Voronoi volume, the packing of residues involved in protein-protein interaction has been compared to that in the protein interior. For a comparable number of atoms the interface has about twice the number of cavities relative to the tertiary structure. |
| first_indexed | 2024-12-21T00:59:58Z |
| format | Article |
| id | doaj.art-65f4c139d24c48b48e15aa6d4cffc895 |
| institution | Directory Open Access Journal |
| issn | 1553-734X 1553-7358 |
| language | English |
| last_indexed | 2024-12-21T00:59:58Z |
| publishDate | 2008-09-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Computational Biology |
| spelling | doaj.art-65f4c139d24c48b48e15aa6d4cffc8952022-12-21T19:21:12ZengPublic Library of Science (PLoS)PLoS Computational Biology1553-734X1553-73582008-09-0149e100018810.1371/journal.pcbi.1000188Cavities and atomic packing in protein structures and interfaces.Shrihari SonavanePinak ChakrabartiA comparative analysis of cavities enclosed in a tertiary structure of proteins and interfaces formed by the interaction of two protein subunits in obligate and non-obligate categories (represented by homodimeric molecules and heterocomplexes, respectively) is presented. The total volume of cavities increases with the size of the protein (or the interface), though the exact relationship may vary in different cases. Likewise, for individual cavities also there is quantitative dependence of the volume on the number of atoms (or residues) lining the cavity. The larger cavities tend to be less spherical, solvated, and the interfaces are enriched in these. On average 15 A(3) of cavity volume is found to accommodate single water, with another 40-45 A(3) needed for each additional solvent molecule. Polar atoms/residues have a higher propensity to line solvated cavities. Relative to the frequency of occurrence in the whole structure (or interface), residues in beta-strands are found more often lining the cavities, and those in turn and loop the least. Any depression in one chain not complemented by a protrusion in the other results in a cavity in the protein-protein interface. Through the use of the Voronoi volume, the packing of residues involved in protein-protein interaction has been compared to that in the protein interior. For a comparable number of atoms the interface has about twice the number of cavities relative to the tertiary structure.http://europepmc.org/articles/PMC2582456?pdf=render |
| spellingShingle | Shrihari Sonavane Pinak Chakrabarti Cavities and atomic packing in protein structures and interfaces. PLoS Computational Biology |
| title | Cavities and atomic packing in protein structures and interfaces. |
| title_full | Cavities and atomic packing in protein structures and interfaces. |
| title_fullStr | Cavities and atomic packing in protein structures and interfaces. |
| title_full_unstemmed | Cavities and atomic packing in protein structures and interfaces. |
| title_short | Cavities and atomic packing in protein structures and interfaces. |
| title_sort | cavities and atomic packing in protein structures and interfaces |
| url | http://europepmc.org/articles/PMC2582456?pdf=render |
| work_keys_str_mv | AT shriharisonavane cavitiesandatomicpackinginproteinstructuresandinterfaces AT pinakchakrabarti cavitiesandatomicpackinginproteinstructuresandinterfaces |