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Application of amino acid distribution along the sequence for discriminating mesophilic and thermophilic proteins

Paper ID Volume ID Publish Year Pages File Format Full-Text
36201 45124 2006 7 PDF Available
Title
Application of amino acid distribution along the sequence for discriminating mesophilic and thermophilic proteins
Abstract

In this work, we have systematically analyzed the distribution of two neighboring amino acids in the sequences of thermophilic and mesophilic proteins. We observed that the occurrence of EE, KK, RR, PP, KI, VV, VE, KE and VK in thermophilic proteins were significantly higher, while the occurrence of QQ, AA, EQ, LL, QA, QL, NN, KQ, QG, RQ, QT and AQ were significantly lower. The thermostable mechanism was studied and we thought that the dipeptide composition contained more information than amino acid composition. Based on the information of dipeptide composition, we have developed a statistical method for discriminating thermophilic and mesophilic proteins. The accuracy of our method for the training dataset was 86.3%. Furthermore, the accuracy of the method for another two independent testing datasets was 85.5 and 89.7%, respectively. The influence of some specific dipeptides on prediction accuracy was also discussed.

Keywords
Dipeptide composition; Amino acid composition; Discrimination; Protein thermostability
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Application of amino acid distribution along the sequence for discriminating mesophilic and thermophilic proteins
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 41, Issue 8, August 2006, Pages 1792–1798
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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