Pattern similarity study of functional sites in protein sequences: lysozymes and cystatins

摘要: Although it is generally agreed that topography more conserved than sequences, proteins sharing the same fold can have different functions, while there are protein families with low sequence similarity. An alternative method for profile analysis of characteristic positions motifs within 3D structures may be needed functional annotation sequences. Using approach quantitative structure-activity relationships (QSAR), we proposed a new algorithm postulating mechanisms on basis pattern similarity and average property values side-chains in segments This was used to search sites belonging lysozyme cystatin families. Hydrophobicity β-turn propensity reference 3–7 residues were homology (HSS) active sites. Hydrogen bonding as side-chain searching binding lysozymes. The profiles constants these parameters functions their sequences could identify both substrate Streptomyces coelicolor, which has been reported enzyme (Cellosyl). successfully applied cystatins, especially amyloidosis human C well lysozyme. Pattern index structure-related properties side chains short three or longer were, first time, predicting applicable studying un-annotated proteins, complete not yet available.