## Abstract In relation to the prediction of allergenicity three aspects have to be discussed: IgE immunogenicity, IgE cross‐reactivity, and T‐cell cross‐reactivity. IgE immunogenicity depends largely on factors other than the protein itself: the context and dose and “history” of the protein by the
In silico prediction of deleterious single amino acid polymorphisms from amino acid sequence
✍ Scribed by Shuyan Li; Lili Xi; Jiazhong Li; Chengqi Wang; Beilei Lei; Yulin Shen; Huanxiang Liu; Xiaojun Yao; Biao Li
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 211 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0192-8651
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✦ Synopsis
Abstract
Molecular cause of human disease retains as one of the most attractive scientific research targets for decades. An effective approach toward this topic is analysis and identification of disease‐related amino acid polymorphisms. In this work, we developed a concise and promising deleterious amino acid polymorphism identification method SeqSubPred based on 44 features solely extracted from protein sequence. SeqSubPred achieved surprisingly good predictive ability with accuracy (0.88) and area under receiver operating characteristic (0.94) without resorting to homology or evolution information, which is frequently used in similar methods and usually more complex and time‐consuming. SeqSubPred also identified several critical sequence features obtained from random forests model, and these features brought some interesting insights into the factors affecting human disease‐related amino acid substitutions. The online version of SeqSubPred method is available at montana.informatics.indiana.edu/cgi‐bin/seqmut/seqsubpred.cgi © 2010 Wiley Periodicals, Inc. J Comput Chem, 2011
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UniProtKB/Swiss-Prot (http://beta.uniprot.org/uniprot; last accessed: 19 October 2007) is a manually curated knowledgebase providing information on protein sequences and functional annotation. It is part of the Universal Protein Resource (UniProt). The knowledgebase currently records a total of 32,2
Having obtained the amino acid composition of a protein, chemists and molecular biologists may wish to identify the protein from this data alone. In general such data will have errors associated with them and the length of the protein may be known only approximately or not at all. In this paper a me