{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/85492"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/85492","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Protein Three -Dimensional Structure: Theoretical and Computational Aspects of Structure Prediction Based on the Amino Acid Sequence","abstract":"Given that the repertoire of secondary structure classifications is limited, we asked if there is a limited set, even if large, of structural features that describe the protein three-dimensional structure adequately. Towards this end, we created libraries of peptide fragments of sizes 7 to 13 respectively and clustered them based on structural similarity. Analysis of these clustered fragments show that these adequately describe the protein structure space. In order to use this paradigm for ab initio structure prediction, we examined sequence-structure relationships in these clusters. It turns out that while structural characterization is nearly complete, the mapping from sequence to structure is not unique and no significant correlations exist between the sequences in a given structural cluster. Examination of numerous protein structures using sequence-structure correlations show that there are regions in proteins which show a degree of correlation. These are perhaps the folding motifs in proteins and this warrants further examination.","abstract_html":"Given that the repertoire of secondary structure classifications is limited, we asked if there is a limited set, even if large, of structural features that describe the protein three-dimensional structure adequately. Towards this end, we created libraries of peptide fragments of sizes 7 to 13 respectively and clustered them based on structural similarity. Analysis of these clustered fragments show that these adequately describe the protein structure space. In order to use this paradigm for ab initio structure prediction, we examined sequence-structure relationships in these clusters. It turns out that while structural characterization is nearly complete, the mapping from sequence to structure is not unique and no significant correlations exist between the sequences in a given structural cluster. Examination of numerous protein structures using sequence-structure correlations show that there are regions in proteins which show a degree of correlation. These are perhaps the folding motifs in proteins and this warrants further examination.","abstract_has_math":false,"creators":["Pappas, Georgios Joannis, Jr"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics and Computational Biology","degree_department":null,"school":null,"contributors":["Subramaniam, Shankar"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:46:16Z","date_published":"2015-09-25T22:46:16Z","updated_at":"2026-07-22T22:26:25Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9944960"],"render_values":[{"text":"(MiAaPQ)AAI9944960","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/85492","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Subramaniam, Shankar"]},{"key":"dc:creator","label":"Author","values":["Pappas, Georgios Joannis, Jr"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:46:16Z","10000-01-01","1999"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics and Computational Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biophysics, General"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/85492","(MiAaPQ)AAI9944960"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Given that the repertoire of secondary structure classifications is limited, we asked if there is a limited set, even if large, of structural features that describe the protein three-dimensional structure adequately. Towards this end, we created libraries of peptide fragments of sizes 7 to 13 respectively and clustered them based on structural similarity. Analysis of these clustered fragments show that these adequately describe the protein structure space. In order to use this paradigm for ab initio structure prediction, we examined sequence-structure relationships in these clusters. It turns out that while structural characterization is nearly complete, the mapping from sequence to structure is not unique and no significant correlations exist between the sequences in a given structural cluster. Examination of numerous protein structures using sequence-structure correlations show that there are regions in proteins which show a degree of correlation. These are perhaps the folding motifs in proteins and this warrants further examination.","Made available in DSpace on 2015-09-25T22:46:16Z (GMT). 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Towards this end, we created libraries of peptide fragments of sizes 7 to 13 respectively and clustered them based on structural similarity. Analysis of these clustered fragments show that these adequately describe the protein structure space. In order to use this paradigm for ab initio structure prediction, we examined sequence-structure relationships in these clusters. It turns out that while structural characterization is nearly complete, the mapping from sequence to structure is not unique and no significant correlations exist between the sequences in a given structural cluster. Examination of numerous protein structures using sequence-structure correlations show that there are regions in proteins which show a degree of correlation. These are perhaps the folding motifs in proteins and this warrants further examination.","Made available in DSpace on 2015-09-25T22:46:16Z (GMT). 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