28th Hawaii International Conference on System Sciences (HICSS'95) Hawaii, USA January 04-January 07 ISBN: 0-8186-6921-7
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.
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, pp.312, 28th Hawaii International Conference on System Sciences (HICSS'95), 1995 Usage of this product signifies your acceptance of the Terms of Use. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||