Skip Navigation


Bioinformatics Advance Access originally published online on September 17, 2004
Bioinformatics 2005 21(2):152-159; doi:10.1093/bioinformatics/bth487
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow All Versions of this Article:
21/2/152    most recent
bth487v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (38)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Lin, K.
Right arrow Articles by Heringa, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lin, K.
Right arrow Articles by Heringa, J.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Bioinformatics vol. 21 issue 2 © Oxford University Press 2005; all rights reserved.

A simple and fast secondary structure prediction method using hidden neural networks

Kuang Lin 1,*,{dagger}, Victor A. Simossis 2,{dagger}, Willam R. Taylor 1 and Jaap Heringa 2,3

1 Division of Mathematical Biology, The National Institute for Medical Research The Ridgeway, Mill Hill, London NW7 1AA, UK
2 Bioinformatics Section, Faculty of Sciences and Faculty of Earth and Life Sciences, Vrije Universiteit Amsterdam De Boelelaan 1081A, 1081 HV Amsterdam, The Netherlands
3 Centre for Integrative Bioinformatics (IBIVU), Faculty of Sciences and Faculty of Earth and Life Sciences, Vrije Universiteit Amsterdam De Boelelaan 1081A, 1081 HV Amsterdam, The Netherlands

*To whom correspondence should be addressed.

Motivation: In this paper, we present a secondary structure prediction method YASPIN that unlike the current state-of-the-art methods utilizes a single neural network for predicting the secondary structure elements in a 7-state local structure scheme and then optimizes the output using a hidden Markov model, which results in providing more information for the prediction.

Results: YASPIN was compared with the current top-performing secondary structure prediction methods, such as PHDpsi, PROFsec, SSPro2, JNET and PSIPRED. The overall prediction accuracy on the independent EVA5 sequence set is comparable with that of the top performers, according to the Q3, SOV and Matthew's correlations accuracy measures. YASPIN shows the highest accuracy in terms of Q3 and SOV scores for strand prediction.

Availability: YASPIN is available on-line at the Centre for Integrative Bioinformatics website (http://ibivu.cs.vu.nl/programs/yaspinwww/) at the Vrije University in Amsterdam and will soon be mirrored on the Mathematical Biology website (http://www.mathbio.nimr.mrc.ac.uk) at the NIMR in London.

Contact: kxlin{at}nimr.mrc.ac.uk


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
BioinformaticsHome page
X. Li, T. Kahveci, and A. M. Settles
A novel genome-scale repeat finder geared towards transposons
Bioinformatics, February 15, 2008; 24(4): 468 - 476.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
K. Chen and L. Kurgan
PFRES: protein fold classification by using evolutionary information and predicted secondary structure
Bioinformatics, November 1, 2007; 23(21): 2843 - 2850.
[Abstract] [Full Text] [PDF]


Home page
Drug Metab. Dispos.Home page
J. M. Walraven, J. O. Trent, and D. W. Hein
Computational and Experimental Analyses of Mammalian Arylamine N-Acetyltransferase Structure and Function
Drug Metab. Dispos., June 1, 2007; 35(6): 1001 - 1007.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
S. Mann, J. Li, and Y.-P. P. Chen
A pHMM-ANN based discriminative approach to promoter identification in prokaryote genomic contexts
Nucleic Acids Res., January 28, 2007; 35(2): e12 - e12.
[Abstract] [Full Text] [PDF]


Home page
Protein Sci.Home page
T. Z. Sen, H. Cheng, A. Kloczkowski, and R. L. Jernigan
A Consensus Data Mining secondary structure prediction by combining GOR V and Fragment Database Mining
Protein Sci., November 1, 2006; 15(11): 2499 - 2506.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
D. Zhang, C. J. Martyniuk, and V. L. Trudeau
SANTA domain: a novel conserved protein module in Eukaryota with potential involvement in chromatin regulation
Bioinformatics, October 15, 2006; 22(20): 2459 - 2462.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
L. S. Garrenton, S. L. Young, and J. Thorner
Function of the MAPK scaffold protein, Ste5, requires a cryptic PH domain
Genes & Dev., July 15, 2006; 20(14): 1946 - 1958.
[Abstract] [Full Text] [PDF]


Home page
Protein Sci.Home page
D. Kihara
The effect of long-range interactions on the secondary structure formation of proteins
Protein Sci., August 1, 2005; 14(8): 1955 - 1963.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
V. A. Simossis and J. Heringa
PRALINE: a multiple sequence alignment toolbox that integrates homology-extended and secondary structure information
Nucleic Acids Res., July 1, 2005; 33(suppl_2): W289 - W294.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.