DocumentCode :
776499
Title :
Folding type specific secondary structure propensities of synonymous codons
Author :
Gu, Wanjun ; Zhou, Tong ; Ma, Jianmin ; Sun, Xiao ; Lu, Zuhong
Author_Institution :
Key Lab. of Molecular & Biomolecular Electron., Southeast Univ., Nanjing, China
Volume :
2
Issue :
3
fYear :
2003
Firstpage :
150
Lastpage :
157
Abstract :
We have proposed new amino acid secondary structure propensities in proteins with different folding types based on synonymous codons. They have been derived from 200 all alpha, all beta, alpha/beta, and alpha + beta proteins of known structures and their coding genes. The secondary structure propensities of the same codon in gene coding for different folding type proteins are not the same. For instance, amino acid Ile coded by AUU is indifferent to form the alpha unit in the alpha + beta protein class, but it is a former and a breaker for the alpha unit in the all alpha protein class and the alpha/beta class, respectively. On the other hand, the secondary structure propensities of different synonymous codons in the coding genes with the same folding type are also not all the same. As an example, CGU, CGG, and AGA, which are synonymous codons of Arg, are preferential to form the alpha unit in all alpha proteins, while CGA is an alpha unit breaker and the other two synonymous codons, CGC and AGG, are indifferent to form or break the alpha unit. As a result, protein secondary structure information contained both in mRNA sequences and in amino acid sequences has been introduced in these codon-based amino acid secondary structure propensities. These codon-based amino acid secondary structure propensities are helpful to in vitro protein design and protein secondary structure prediction.
Keywords :
genetics; molecular biophysics; molecular configurations; proteins; AGA; Arg; CGA; CGG; alpha unit; beta protein; coding genes; folding type specific secondary structure propensities; in vitro protein design; protein secondary structure prediction; synonymous codons; Accuracy; Amino acids; Application specific processors; In vitro; Molecular electronics; Organisms; Prediction methods; Protein engineering; Protein sequence; Sun; Amino Acid Sequence; Amino Acids; Base Sequence; Codon; Models, Chemical; Models, Molecular; Molecular Sequence Data; Protein Folding; Protein Structure, Secondary; Proteins; Sequence Alignment; Sequence Analysis; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid;
fLanguage :
English
Journal_Title :
NanoBioscience, IEEE Transactions on
Publisher :
ieee
ISSN :
1536-1241
Type :
jour
DOI :
10.1109/TNB.2003.817024
Filename :
1229599
Link To Document :
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