Home

About

Advanced Search

Browse by Discipline

Scientific Societies

E-print Alerts

Add E-prints

E-print Network
FAQHELPSITE MAPCONTACT US


  Advanced Search  

 
PROTEIN FOLD RECOGNITION USING RESIDUE-BASED ALIGNMENTS OF SEQUENCE AND SECONDARY STRUCTURE
 

Summary: PROTEIN FOLD RECOGNITION USING RESIDUE-BASED ALIGNMENTS OF SEQUENCE
AND SECONDARY STRUCTURE
Zafer Aydin*, Hakan Erdogan**, and Yucel Altunbasak*
*Center for Signal and Image Processing,
Centergy 5th floor, Georgia Institute ofTechnology
Atlanta, GA 30332-0250
E-mail:{aydinz,yucel} d)ece.gatech.edu
ABSTRACT
Protein structure prediction aims to determine the three-dimensional
structure of proteins form their amino acid sequences. When a pro-
tein does not have similarity (homology) to any known fold, thread-
ing or fold recognition methods are used to predict structure. Fold
recognition methods frequently employ secondary structure, solvent
accessibility, and evolutionary information to enhance the accuracy
and the quality ofthe predictions.
In this paper, we present a residue based alignment method as
an alternative to the state-of-the-art SSEA method, originally intro-
duced by Przytycka et al. [1], and further modified by McGuffin
et al. [2]. We introduce a residue-based score function, which can
incorporate amino acid similarity matrices such as BLOSUM into

  

Source: Aydin, Zafer - Department of Genome Sciences, University of Washington at Seattle
Erdogan, Hakan - Faculty of Engineering and Natural Sciences, Sabanci University

 

Collections: Biology and Medicine; Energy Storage, Conversion and Utilization