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Published Articles >> Table of Contents >> Abstract
28th Hawaii International Conference on System Sciences (HICSS'95)
p. 312
The pattern of common supersecondary structure (motifs) in protein database
Zhirong Sun, Dept. of Biol. Sci. & Biotechnol., Tsinghua Univ., Beijing, China
T. Blundell, Dept. of Biol. Sci. & Biotechnol., Tsinghua Univ., Beijing, China
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DOI Bookmark: http://doi.ieeecomputersociety.org/10.1109/HICSS.1995.375325
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| Abstract |
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Supersecondary motifs have been analysed in 240 proteins defined at resolutions of 0.25 nm or better. Using five classes of residue conformation (a,b,e,l,t) in the non-regular structure regions, we have identified 50 classes that occur at least five times, and eleven classes that occur more than twenty-five times. The sequence pattern of the eleven most frequently occurring motifs have been characterised. The results should be useful for homology modelling and structure prediction.
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 Additional Information
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Index Terms- proteins; biology computing; chemistry computing; database management systems; common supersecondary structure; motifs; protein database; supersecondary motifs; proteins; residue conformation; nonregular structure regions; sequence pattern; homology modelling; structure prediction
Citation:
Zhirong Sun, T. Blundell,
"The pattern of common supersecondary structure (motifs) in protein database,"
hicss,
p. 312,
28th Hawaii International Conference on System Sciences (HICSS'95),
1995
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