Abstract

A protein's properties are influenced by both its amino-acid sequence and its three-dimensional conformation. Ascertaining a protein's sequence is relatively easy using modern techniques, but determining its conformation requires much more expensive and time-consuming techniques. Consequently, it would be useful to identify a method that can accurately predict a protein's secondary-structure conformation using only the protein's sequence data. This problem is not trivial, however, because identical amino-acid subsequences in different contexts sometimes have disparate secondary structures, while highly dissimilar amino-acid subsequences sometimes have identical secondary structures. We propose (1) to develop a set of metrics that facilitates better comparisons between dissimilar subsequences and (2) to design a custom set of inputs for machine-learning models that can harness contextual dependence information between the secondary structures of successive amino acids in order to achieve better secondary-structure prediction accuracy.

Degree

MS

College and Department

Physical and Mathematical Sciences; Computer Science

Rights

http://lib.byu.edu/about/copyright/

Date Submitted

2015-05-01

Document Type

Thesis

Handle

http://hdl.lib.byu.edu/1877/etd8506

Language

english

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