Faculty Publications

Optimizing The Size Of The Sequence Profiles To Increase The Accuracy Of Protein Sequence Alignments Generated By Profile-Profile Algorithms

Document Type

Article

Journal/Book/Conference Title

Bioinformatics

Volume

24

Issue

9

First Page

1145

Last Page

1153

Abstract

Motivation: Profile-based protein homology detection algorithms are valuable tools in genome annotation and protein classification. By utilizing information present in the sequences of homologous proteins, profile-based methods are often able to detect extremely weak relationships between protein sequences, as evidenced by the large-scale benchmarking experiments such as CASP and LiveBench. Results: We study the relationship between the sensitivity of a profile-profile method and the size of the sequence profile, which is defined as the average number of different residue types observed at the profile's positions. We also demonstrate that improvements in the sensitivity of a profile-profile method can be made by incorporating a profile-dependent scoring scheme, such as position-specific background frequencies. The techniques presented in this article are implemented in an alignment algorithm UNI-FOLD. When tested against other well-established methods for fold recognition, UNI-FOLD shows increased sensitivity and specificity in detecting remote relationships between protein sequences. © The Author 2008. Published by Oxford University Press. All rights reserved.

Department

Department of Computer Science

Original Publication Date

5-1-2008

DOI of published version

10.1093/bioinformatics/btn097

Link to Full Text

Comments?

Share

COinS