Principle component analysis in F/10 and G/11 xylanase.
A bioinformatics method was used to analyze F/10 and G/11 xylanase basing on principle component analysis, and a model was made to classify between these two folds with an ideal result. The principle components were predicated to be secondary structures, the components were analyzed with the architecture of each family, and found comparable with (beta/alpha)(8)-barrel of F/10 xylanase and right-hand structure of G/11 xylanase. Compared with sequence similarities, this method gave discriminating features a clear meaning. The largest component did not appear in the model, which revealed no difference between these two families.
The Key Laboratory of Industrial Biotechnology, Ministry of Education, Southern Yangtze University, 170 Huihe Road, Wuxi 214036, Jiangsu, PR China. llw321@yahoo.com.cn
Liangwei
L
Liu
Jue
J
Zhang
Bin
B
Chen
Weilan
W
Shao
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D003198:Computer Simulation; D030562:Databases, Protein; D043364:Endo-1,4-beta Xylanases / Q000032:analysis / Q000737:chemistry* / Q000145:classification*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D025341:Principal Component Analysis; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D020539:Sequence Analysis, Protein / Q000379:methods*; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D043364:Endo-1,4-beta Xylanases