Optimization of profile-to-profile alignment parameters for one-dimensional threading.
The development of automatic approaches for the comparison of protein sequences has become increasingly important. Methods that compare profiles allow for the use of information about whole protein families, resulting in more sensitive and accurate detection of distantly related sequences. In this contribution, we describe a thorough optimization and tests of a profile-to-profile alignment method. A number of different scoring schemes has been implemented and compared on the basis of their ability to identify a template protein from the same SCOP family as a query. In addition to sequence profiles, secondary structure profiles were used to increase the rate of successful detection. Our results show that a properly tuned one-dimensional threading method can recognize a correct template from the same SCOP family nearly as well as structural alignment. Our benchmark set, which might be useful in other similar studies, as well as the fold-recognition software we developed may be downloaded (www.bioshell.pl/profile-alignments).
Faculty of Chemistry, Warsaw University, Warsaw, Poland.
Pawel
P
Gniewek
Andrzej
A
Kolinski
Dominik
D
Gront
D000465:Algorithms; D030562:Databases, Protein; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D012984:Software; D040681:Structural Homology, Protein
D011506:Proteins