DocumentCode :
1153533
Title :
Multiple alignment through protein secondary-structure information
Author :
Armano, Giuliano ; Milanesi, Luciano ; Orro, Alessandro
Author_Institution :
Dept. of Electr. & Electron. Eng., Univ. of Cagliari, Italy
Volume :
4
Issue :
3
fYear :
2005
Firstpage :
207
Lastpage :
211
Abstract :
It is well known that protein secondary-structure information can help the process of performing multiple alignment, in particular when the amount of similarity among the involved sequences moves toward the "twilight zone" (less than 30% of pairwise similarity). In this paper, a multiple alignment algorithm is presented, explicitly designed for exploiting any available secondary-structure information. A layered architecture with two interacting levels has been defined for dealing with both primary- and secondary-structure information of target sequences. Secondary structure (either available or predicted by resorting to a technique based on multiple experts) is used to calculate an initial alignment at the secondary level, to be arranged by locally scoped operators devised to refine the alignment at the primary level. Aimed at evaluating the impact of secondary information on the quality of alignments, in particular alignments with a low degree of similarity, the technique has been implemented and assessed on relevant test cases.
Keywords :
molecular biophysics; molecular configurations; proteins; protein multiple alignment; protein secondary structure; protein sequences; Algorithm design and analysis; Bioinformatics; Biomedical engineering; Cost function; Dynamic programming; Genomics; Matrices; Organisms; Proteins; Testing; Protein multiple alignment; protein secondary-structure prediction; Algorithms; Amino Acid Sequence; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Proteins; Sequence Alignment; Sequence Analysis, Protein; Sequence Homology, Amino Acid;
fLanguage :
English
Journal_Title :
NanoBioscience, IEEE Transactions on
Publisher :
ieee
ISSN :
1536-1241
Type :
jour
DOI :
10.1109/TNB.2005.853644
Filename :
1501837
Link To Document :
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