Please use this identifier to cite or link to this item: http://cmuir.cmu.ac.th/jspui/handle/6653943832/49705
Title: Prediction of the disulphide bonding state of cysteines in proteins using Conditional Random Fields
Authors: Watshara Shoombuatong
Patrinee Traisathit
Sukon Prasitwattanaseree
Chatchai Tayapiwatana
Robert Cutler
Jeerayut Chaijaruwanich
Keywords: Biochemistry, Genetics and Molecular Biology
Computer Science
Social Sciences
Issue Date: 1-Jul-2011
Abstract: The formation of disulphide bonds between cysteines plays a major role in protein folding, structure, function and evolution. Many computational approaches have been used to predict the disulphide bonding state of cysteines. In our work, we developed a novel method based on Conditional Random Fields (CRFs) to predict the disulphide bonding state from protein primary sequence, predicted secondary structures and predicted relative solvent accessibilities (all-state information). Our experiments obtain 84% accuracy, 88% precision and 94% recall, using all-state information. However, our results show essentially identical results when using protein sequence and predicted relative solvent accessibilities in the absence of secondary structure. © 2011 Inderscience Enterprises Ltd.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79960970337&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/49705
ISSN: 17485681
17485673
Appears in Collections:CMUL: Journal Articles

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