Dissertations and Theses @ UNI
Availability
Open Access Thesis
Keywords
Protein-protein interactions; Proteins--Conformation; Academic theses;
Abstract
Structural alignment is an important tool for identifying structural and functional relationships between proteins. A typical protein structure alignment method is an iterative algorithm that computes an optimal residue-residue correspondence, once for each inspected spatial superposition of the input proteins. The significance of this study allows us to better understand how important it is to explore in deep the analysis of proteins structure using a residue pair distance as the way to align two proteins. We assess the extent of improvements in the accuracy of the existing methods that can be made by exploring the search space in a more detailed manner. As part of this study, we carried out two benchmarks. In the first benchmark, the improvement in the accuracies of three well known algorithms for protein structure comparison is assessed using a set of reference alignments generated by experts in the field. The second benchmark utilizes a set of commonly accepted measures of protein structure alignment quality.
Year of Submission
2011
Degree Name
Master of Science
Department
Department of Computer Science
First Advisor
Aleksandar Poleksic
Second Advisor
Mark A. Fineup
Third Advisor
Michael H. Walter
Date Original
2011
Object Description
1 PDF file (46 leaves)
Copyright
©2011 Mauricio J. Arrigada-Benitez
Language
en
File Format
application/pdf
Recommended Citation
Arriagada-Benitez, Mauricio J., "Increasing the Accuracy of Protein Three-Dimensional Structure Comparison" (2011). Dissertations and Theses @ UNI. 1957.
https://scholarworks.uni.edu/etd/1957
Comments
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