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Massachusetts Institute of Technology

Mathematical methods for protein structural motif recognition

Abstract

dc:description.abstract

In this thesis, two algorithms for protein structural motif recognition are presented. A program is described which successfully recognizes the occurrence of the right-handed parallel 8-helix fold from protein sequence data alone. When run on sequences of unknown structure the program identifies the fold in a significant number of microbial outer membrane and cell-surface proteins implicated in infectious disease. A search algorithm is introduced for unsupervised discovery of protein sequence patterns that are significantly correlated with structural motifs. The algorithm identifies known, biologically relevant patterns as well as several potentially novel motifs. It is hoped that both algorithms may contribute to a better understanding of the connection between protein sequence and structure.

Degree

thesis:*
Department dc:contributor.department
Massachusetts Institute of Technology. Dept. of Mathematics.
Grantor dc:publisher
Massachusetts Institute of Technology
Year dc:date.issued
2001

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Bradley, Philip H. (Philip Harlan), 1973-
Advisor dc:contributor.advisor
  • Bonnie Berger.

Subjects

dc:subject × 1

Rights

dc:rights
Statement dc:rights
  • M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.
Language dc:language.iso
eng

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/1721.1/8641
OAI identifier oai:identifier
oai:dspace.mit.edu:1721.1/8641

Chain of custody

source
Harvested from
MIT
Base URL
dspace.mit.edu/oai/request
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
related terms
citation

Bradley, Philip H. (Philip Harlan), 1973-. Mathematical methods for protein structural motif recognition. Massachusetts Institute of Technology, 2001. http://hdl.handle.net/1721.1/8641