A novel index of protein-protein interface propensity improves interface residue recognition. Issue 4 (December 2016)
- Record Type:
- Journal Article
- Title:
- A novel index of protein-protein interface propensity improves interface residue recognition. Issue 4 (December 2016)
- Main Title:
- A novel index of protein-protein interface propensity improves interface residue recognition
- Authors:
- Dai, Wentao
Wu, Aiping
Ma, Liangxiao
Li, Yi-Xue
Jiang, Taijiao
Li, Yuan-Yuan - Abstract:
- Abstract Background Protein-protein interface holds important information of protein-protein interactions which play key roles in most biological processes. In the past few years, a lot of efforts have been made to improve interface residue recognition by characterizing protein-protein interfaces and extracting relevant features. However, most previous studies were carried out in a qualitative level, and there are also some inconsistencies between them. Results In the present work, to improve interface residue recognition, we built a novel quantitative residue protein-protein interface propensity index (QIPI) and gained a comprehensive picture of protein-protein interface through analyzing protein-protein interfaces on our comprehensive protein-protein interfaces dataset (Astral2.05-40-4506). Furthermore, in order to assess the effect of QIPI in improving the protein-protein interface prediction, we developed an interface residue recognition method SPR (Single domain based Patch Recognition) based on the QIPI. The evaluation results proved that our novel QIPI is able to improve the interface residue recognition. Conclusions Through a comprehensive quantitative analysis of protein-protein interface, we constructed a novel quantitative protein-protein interface propensity index (QIPI), which could be easily applied to improve the interface residue recognition and helpful in understanding the protein-protein interface. Availability QIPI and SPR are available to non-commercialAbstract Background Protein-protein interface holds important information of protein-protein interactions which play key roles in most biological processes. In the past few years, a lot of efforts have been made to improve interface residue recognition by characterizing protein-protein interfaces and extracting relevant features. However, most previous studies were carried out in a qualitative level, and there are also some inconsistencies between them. Results In the present work, to improve interface residue recognition, we built a novel quantitative residue protein-protein interface propensity index (QIPI) and gained a comprehensive picture of protein-protein interface through analyzing protein-protein interfaces on our comprehensive protein-protein interfaces dataset (Astral2.05-40-4506). Furthermore, in order to assess the effect of QIPI in improving the protein-protein interface prediction, we developed an interface residue recognition method SPR (Single domain based Patch Recognition) based on the QIPI. The evaluation results proved that our novel QIPI is able to improve the interface residue recognition. Conclusions Through a comprehensive quantitative analysis of protein-protein interface, we constructed a novel quantitative protein-protein interface propensity index (QIPI), which could be easily applied to improve the interface residue recognition and helpful in understanding the protein-protein interface. Availability QIPI and SPR are available to non-commercial users at our website:http://www.scbit.org/QIPI/ . … (more)
- Is Part Of:
- BMC systems biology. Volume 10:Issue 4(2016)
- Journal:
- BMC systems biology
- Issue:
- Volume 10:Issue 4(2016)
- Issue Display:
- Volume 10, Issue 4 (2016)
- Year:
- 2016
- Volume:
- 10
- Issue:
- 4
- Issue Sort Value:
- 2016-0010-0004-0000
- Page Start:
- 381
- Page End:
- 392
- Publication Date:
- 2016-12
- Subjects:
- Biological systems -- Periodicals
Biology -- Research -- Periodicals
Cell physiology -- Periodicals
Genes -- Analysis -- Periodicals
571 - Journal URLs:
- http://www.biomedcentral.com/bmcsystbiol/ ↗
http://link.springer.com/ ↗ - DOI:
- 10.1186/s12918-016-0351-7 ↗
- Languages:
- English
- ISSNs:
- 1752-0509
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 10954.xml