Cargando…
Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins
BACKGROUND: We describe Distill, a suite of servers for the prediction of protein structural features: secondary structure; relative solvent accessibility; contact density; backbone structural motifs; residue contact maps at 6, 8 and 12 Angstrom; coarse protein topology. The servers are based on lar...
Autores principales: | , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2006
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1574355/ https://www.ncbi.nlm.nih.gov/pubmed/16953874 http://dx.doi.org/10.1186/1471-2105-7-402 |
_version_ | 1782130293777367040 |
---|---|
author | Baú, Davide Martin, Alberto JM Mooney, Catherine Vullo, Alessandro Walsh, Ian Pollastri, Gianluca |
author_facet | Baú, Davide Martin, Alberto JM Mooney, Catherine Vullo, Alessandro Walsh, Ian Pollastri, Gianluca |
author_sort | Baú, Davide |
collection | PubMed |
description | BACKGROUND: We describe Distill, a suite of servers for the prediction of protein structural features: secondary structure; relative solvent accessibility; contact density; backbone structural motifs; residue contact maps at 6, 8 and 12 Angstrom; coarse protein topology. The servers are based on large-scale ensembles of recursive neural networks and trained on large, up-to-date, non-redundant subsets of the Protein Data Bank. Together with structural feature predictions, Distill includes a server for prediction of C(α )traces for short proteins (up to 200 amino acids). RESULTS: The servers are state-of-the-art, with secondary structure predicted correctly for nearly 80% of residues (currently the top performance on EVA), 2-class solvent accessibility nearly 80% correct, and contact maps exceeding 50% precision on the top non-diagonal contacts. A preliminary implementation of the predictor of protein C(α )traces featured among the top 20 Novel Fold predictors at the last CASP6 experiment as group Distill (ID 0348). The majority of the servers, including the C(α )trace predictor, now take into account homology information from the PDB, when available, resulting in greatly improved reliability. CONCLUSION: All predictions are freely available through a simple joint web interface and the results are returned by email. In a single submission the user can send protein sequences for a total of up to 32k residues to all or a selection of the servers. Distill is accessible at the address: . |
format | Text |
id | pubmed-1574355 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-15743552006-09-26 Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins Baú, Davide Martin, Alberto JM Mooney, Catherine Vullo, Alessandro Walsh, Ian Pollastri, Gianluca BMC Bioinformatics Software BACKGROUND: We describe Distill, a suite of servers for the prediction of protein structural features: secondary structure; relative solvent accessibility; contact density; backbone structural motifs; residue contact maps at 6, 8 and 12 Angstrom; coarse protein topology. The servers are based on large-scale ensembles of recursive neural networks and trained on large, up-to-date, non-redundant subsets of the Protein Data Bank. Together with structural feature predictions, Distill includes a server for prediction of C(α )traces for short proteins (up to 200 amino acids). RESULTS: The servers are state-of-the-art, with secondary structure predicted correctly for nearly 80% of residues (currently the top performance on EVA), 2-class solvent accessibility nearly 80% correct, and contact maps exceeding 50% precision on the top non-diagonal contacts. A preliminary implementation of the predictor of protein C(α )traces featured among the top 20 Novel Fold predictors at the last CASP6 experiment as group Distill (ID 0348). The majority of the servers, including the C(α )trace predictor, now take into account homology information from the PDB, when available, resulting in greatly improved reliability. CONCLUSION: All predictions are freely available through a simple joint web interface and the results are returned by email. In a single submission the user can send protein sequences for a total of up to 32k residues to all or a selection of the servers. Distill is accessible at the address: . BioMed Central 2006-09-05 /pmc/articles/PMC1574355/ /pubmed/16953874 http://dx.doi.org/10.1186/1471-2105-7-402 Text en Copyright © 2006 Baú et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Software Baú, Davide Martin, Alberto JM Mooney, Catherine Vullo, Alessandro Walsh, Ian Pollastri, Gianluca Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins |
title | Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins |
title_full | Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins |
title_fullStr | Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins |
title_full_unstemmed | Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins |
title_short | Distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins |
title_sort | distill: a suite of web servers for the prediction of one-, two- and three-dimensional structural features of proteins |
topic | Software |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1574355/ https://www.ncbi.nlm.nih.gov/pubmed/16953874 http://dx.doi.org/10.1186/1471-2105-7-402 |
work_keys_str_mv | AT baudavide distillasuiteofwebserversforthepredictionofonetwoandthreedimensionalstructuralfeaturesofproteins AT martinalbertojm distillasuiteofwebserversforthepredictionofonetwoandthreedimensionalstructuralfeaturesofproteins AT mooneycatherine distillasuiteofwebserversforthepredictionofonetwoandthreedimensionalstructuralfeaturesofproteins AT vulloalessandro distillasuiteofwebserversforthepredictionofonetwoandthreedimensionalstructuralfeaturesofproteins AT walshian distillasuiteofwebserversforthepredictionofonetwoandthreedimensionalstructuralfeaturesofproteins AT pollastrigianluca distillasuiteofwebserversforthepredictionofonetwoandthreedimensionalstructuralfeaturesofproteins |