ACM Home Page
Please provide us with feedback. Feedback
Weave amino acid sequences for protein secondary structure prediction
Full text PdfPdf (161 KB)
Source Data Mining And Knowledge Discovery archive
Proceedings of the 8th ACM SIGMOD workshop on Research issues in data mining and knowledge discovery table of contents
San Diego, California
SESSION: Bioinformatics table of contents
Pages: 80 - 87  
Year of Publication: 2003
Authors
Xiaochun Yang  Brigham Young University, Provo, Utah
Bin Wang  Northeastern University, Shenyang, China.P.R.
Sponsor
SIGMOD: ACM Special Interest Group on Management of Data
Publisher
ACM  New York, NY, USA
Bibliometrics
Downloads (6 Weeks): 1,   Downloads (12 Months): 49,   Citation Count: 0
Additional Information:

abstract   references   index terms   collaborative colleagues   peer to peer  

Tools and Actions: Review this Article  
Save this Article to a Binder    Display Formats: BibTex  EndNote ACM Ref   
DOI Bookmark: Use this link to bookmark this Article: http://doi.acm.org/10.1145/882082.882100
What is a DOI?

ABSTRACT

Given a known protein sequence, predicting its secondary structure can help understand its three-dimensional (tertiary) structure, i.e., the folding. In this paper, we present an approach for predicting protein secondary structures. Different from the existing prediction methods, our approach proposes an encoding schema that weaves physio-chemical information in encoded vectors and a prediction framework that combines the context information with secondary structure segments. We employed Support Vector Machine (SVM) for training the CB513 and RS126 data sets, which are collections of protein secondary structure sequences, through sevenfold cross validation to uncover the structural differences of protein secondary structures. Hereafter, we apply the sliding window technique to test a set of protein sequences based on the group classification learned from the training set. Our approach achieves 77.8% segment overlap accuracy (SOV) and 75.2% three-state overall per-residue accuracy (Q3), which outperform other prediction methods.


REFERENCES

Note: OCR errors may be found in this Reference List extracted from the full text article. ACM has opted to expose the complete List rather than only correct and linked references.

 
1
P. D. Bank. http://www.rcsb.org/pdb/, 2002.
 
2
C.-C. Chang and C.-J. Lin. LIBSVM: a Library for Support Vector Machines. Software available at http://www.csie.ntu.edu.tw/~cjlin/libsvm, 2001.
 
3
J. A. Cuff and G. J. Barton. Evaluation and Improvement of Multiple Sequence Methods for Protein Secondary Structure Prediction. Proteins: Struct. Funct. Genet., 34:508--519, 1999.
 
4
H. Drucker, D. Wu, and V. Vapnik. Support Vector Machines for Span Categorization. IEEE Trans. on Neural Networks, 10:1048--1054, 1999.
 
5
M. O. D. (ed). Atlas of Protein Sequence and Structure. National Biomedical Research Foundation (Washington, D. C.), 5, 1972.
 
6
D. Frishman and P. Argos. Knowledge-Based Protein Secondary Structure Assignment. Proteins, 23:566--579, 1995.
 
7
S. Hua and Z. Sun. A. Novel Method of Protein Secondary Structure Prediction with High Segment Overlap Measure: Support Vector Machine Approach. Bioinformatics, 308:397--407, 2001.
 
8
J. Garnier, D. J. Osguthorpe, and B. Robson. Analysis of the Accuracy and Implications of Simple Methods for Predicting the Secondary Structure of Globular Proteins. J. Mol Biol, 120:97--120, 1978.
 
9
W. Kabsch and C. Sander. A Dictionary of Protein Secondary Structure. Biopolymers, 22:2577--2637, 1983.
 
10
J. Moult and et al. Critical Assessment of Methods of Protein Structure Prediction (CASP): Round II. Proteins. supplement 1., 29(S1):2--6, 1997.
 
11
D. Nelson and M. Cox. Lehninger Principles of Biochemistry Amino. Worth Publishers, 2000.
 
12
 
13
N. Qian and T. J. Sejnowski. Predicting the Secondary Structure of Globular Proteins Using Neural Network Models. J. Mol. Biol, 202:865--884, 1988.
 
14
H. H. Rashidi and K. L. Buehler. Bioinformatics Basics Applications in Biological Science and Medicine. CRC Press, 2000.
 
15
F. M. Richards and C. E. Kundrot. Identification of Structural Motifs from Protein Coordinate Data: Secondary Structure and First-Level Supersecondary Structure. Proteins, 3:71--84, 1988.
 
16
B. Rost and C. Sander. Prediction of Protein Secondary Structure at Better Than 70% Accuracy. J. Mol Biol, 232:584--599, 1993.
 
17
B. Rost, C. Sander, and R. Schneider. Redefining the Goals of Protein Secondary Structure Prediction. J. Mol Biol, 235:13--26, 1994.
 
18
 
19
M. J. Zvelebil, G. J. Barton, W. R. Taylor, and et al. Prediction of Protein Secondary Structure and Active Sites Using the Alignment of Homologous Sequences. J. Mol Biol, 195:957--961, 1987.
 
20
D. Zwillinger, S. G. Krantz, and K. H. Rosen, editors. Standard Mathematical Tables and Formulae (30th edition). CRC Press, 1996.


Peer to Peer - Readers of this Article have also read: