Critical assessment of methods of protein structure prediction (CASP)—Round XII. (15th December 2017)
- Record Type:
- Journal Article
- Title:
- Critical assessment of methods of protein structure prediction (CASP)—Round XII. (15th December 2017)
- Main Title:
- Critical assessment of methods of protein structure prediction (CASP)—Round XII
- Authors:
- Moult, John
Fidelis, Krzysztof
Kryshtafovych, Andriy
Schwede, Torsten
Tramontano, Anna - Abstract:
- Abstract: This article reports the outcome of the 12th round of Critical Assessment of Structure Prediction (CASP12), held in 2016. CASP is a community experiment to determine the state of the art in modeling protein structure from amino acid sequence. Participants are provided sequence information and in turn provide protein structure models and related information. Analysis of the submitted structures by independent assessors provides a comprehensive picture of the capabilities of current methods, and allows progress to be identified. This was again an exciting round of CASP, with significant advances in 4 areas: (i) The use of new methods for predicting three‐dimensional contacts led to a two‐fold improvement in contact accuracy. (ii) As a consequence, model accuracy for proteins where no template was available improved dramatically. (iii) Models based on a structural template showed overall improvement in accuracy. (iv) Methods for estimating the accuracy of a model continued to improve. CASP continued to develop new areas: (i) Assessing methods for building quaternary structure models, including an expansion of the collaboration between CASP and CAPRI. (ii) Modeling with the aid of experimental data was extended to include SAXS data, as well as again using chemical cross‐linking information. (iii) A team of assessors evaluated the suitability of models for a range of applications, including mutation interpretation, analysis of ligand binding properties, andAbstract: This article reports the outcome of the 12th round of Critical Assessment of Structure Prediction (CASP12), held in 2016. CASP is a community experiment to determine the state of the art in modeling protein structure from amino acid sequence. Participants are provided sequence information and in turn provide protein structure models and related information. Analysis of the submitted structures by independent assessors provides a comprehensive picture of the capabilities of current methods, and allows progress to be identified. This was again an exciting round of CASP, with significant advances in 4 areas: (i) The use of new methods for predicting three‐dimensional contacts led to a two‐fold improvement in contact accuracy. (ii) As a consequence, model accuracy for proteins where no template was available improved dramatically. (iii) Models based on a structural template showed overall improvement in accuracy. (iv) Methods for estimating the accuracy of a model continued to improve. CASP continued to develop new areas: (i) Assessing methods for building quaternary structure models, including an expansion of the collaboration between CASP and CAPRI. (ii) Modeling with the aid of experimental data was extended to include SAXS data, as well as again using chemical cross‐linking information. (iii) A team of assessors evaluated the suitability of models for a range of applications, including mutation interpretation, analysis of ligand binding properties, and identification of interfaces. This article describes the experiment and summarizes the results. The rest of this special issue of PROTEINS contains papers describing CASP12 results and assessments in more detail. … (more)
- Is Part Of:
- Proteins. Volume 86(2017)Supplement 1
- Journal:
- Proteins
- Issue:
- Volume 86(2017)Supplement 1
- Issue Display:
- Volume 86, Issue 1 (2017)
- Year:
- 2017
- Volume:
- 86
- Issue:
- 1
- Issue Sort Value:
- 2017-0086-0001-0000
- Page Start:
- 7
- Page End:
- 15
- Publication Date:
- 2017-12-15
- Subjects:
- CASP -- community wide experiment -- protein structure prediction
Proteins -- Periodicals
Proteins -- Periodicals
572.6 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/prot.25415 ↗
- Languages:
- English
- ISSNs:
- 0887-3585
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.164000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 5917.xml