Biology – Quantitative Biology – Biomolecules
Scientific paper
2011-10-28
Biology
Quantitative Biology
Biomolecules
6 pages, 5 figures. Program ProteinEncoder and detailed data are freely available at http://www.genocript.com
Scientific paper
Motivation: Proteins are known to undergo conformational changes in the course of their functions. The changes in conformation are often attributable to a small fraction of residues within the protein. Therefore identification of these variable regions is important for an understanding of protein function. Results: We propose a novel method for identification of local conformational changes in proteins. In our method, backbone conformations are encoded into a sequence of letters from a 16-letter alphabet (called D2 codes) to perform structural comparison. Since we do not use clustering analysis to encode local structures, the D2 codes not only provides a intuitively understandable description of protein structures, but also covers wide varieties of distortions. This paper shows that the D2 codes are better correlated with changes in the dihedral angles than a structural alphabet and a secondary structure description. In the case of the N37S mutant of HIV-1 protease, local conformational changes were captured by the D2 coding method more accurately than other methods. The D2 coding also provided a reliable representation of the difference between NMR models of an HIV-1 protease mutant.
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