{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/25315"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/25315","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Spin lattice relaxation studies on iron proteins","abstract":"The fractal model relating protein structure and vibrational dynamics is reviewed and refined. The temperature dependence of electron spin-lattice relaxation stimulated by Raman phonon scattering is measured in low spin ferric proteins. The data are analysed to yield the spectral dimension, a parameter characterizing the protein vibrational dynamics. Protein X-ray coordinate s are used to approximate a static structural parameter, the fractal dimension. These parameters are related as scaling exponents using simple physical arguments and experimental results. Central issues addressed are the domain of length scales over which the tabulated fractal dimension is a valid scaling exponent and the frequency range of protein vibrations contributing to the measurement of the spectral dimension. Recent experimental findings are interpreted to relate these regimes. They reveal a transition in the spectral dimension from reflecting the protein structure above 6K, to that of the surrounding solvent below this temperature.","abstract_html":"The fractal model relating protein structure and vibrational dynamics is reviewed and refined. The temperature dependence of electron spin-lattice relaxation stimulated by Raman phonon scattering is measured in low spin ferric proteins. The data are analysed to yield the spectral dimension, a parameter characterizing the protein vibrational dynamics. Protein X-ray coordinate s are used to approximate a static structural parameter, the fractal dimension. These parameters are related as scaling exponents using simple physical arguments and experimental results. Central issues addressed are the domain of length scales over which the tabulated fractal dimension is a valid scaling exponent and the frequency range of protein vibrations contributing to the measurement of the spectral dimension. Recent experimental findings are interpreted to relate these regimes. They reveal a transition in the spectral dimension from reflecting the protein structure above 6K, to that of the surrounding solvent below this temperature.","abstract_has_math":false,"creators":["Colvin, John Trevor"],"institution":null,"degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Physics","degree_department":null,"school":null,"contributors":["Stapleton, H.J."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-06-07T15:02:29Z","date_published":"2011-06-07T15:02:29Z","updated_at":"2026-07-22T22:25:24Z","subjects":["electron spin-lattice relaxation","low spin iron proteins","protein structure","vibrational dynamics","Raman phonon scattering"],"languages":["en"],"rights":["1984 John Trevor Colvin"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["826562"],"render_values":[{"text":"826562","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/25315","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Stapleton, H.J."]},{"key":"dc:creator","label":"Author","values":["Colvin, John Trevor"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-06-07T15:02:29Z","10000-01-01","1984"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation / Thesis","text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Physics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["electron spin-lattice relaxation","low spin iron proteins","protein structure","vibrational dynamics","Raman phonon scattering"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["1984 John Trevor Colvin"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["826562","http://hdl.handle.net/2142/25315"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The fractal model relating protein structure and vibrational dynamics is reviewed and refined. The temperature dependence of electron spin-lattice relaxation stimulated by Raman phonon scattering is measured in low spin ferric proteins. The data are analysed to yield the spectral dimension, a parameter characterizing the protein vibrational dynamics. Protein X-ray coordinate s are used to approximate a static structural parameter, the fractal dimension. These parameters are related as scaling exponents using simple physical arguments and experimental results. Central issues addressed are the domain of length scales over which the tabulated fractal dimension is a valid scaling exponent and the frequency range of protein vibrations contributing to the measurement of the spectral dimension. Recent experimental findings are interpreted to relate these regimes. They reveal a transition in the spectral dimension from reflecting the protein structure above 6K, to that of the surrounding solvent below this temperature.","Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-07T15:02:29Z No. of bitstreams: 1 1984_colvin.pdf: 3659139 bytes, checksum: 93bed8c1c0e9b1258f4e1b9ff5cf675a (MD5)","Made available in DSpace on 2011-06-07T15:02:29Z (GMT). No. of bitstreams: 1 1984_colvin.pdf: 3659139 bytes, checksum: 93bed8c1c0e9b1258f4e1b9ff5cf675a (MD5) Previous issue date: 1984","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-06-07T15:02:30Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:13:17-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis","Thesis","U of I Only"]},{"key":"dc:title","label":"Title","values":["Spin lattice relaxation studies on iron proteins"]}]}],"canonical_facts":{"dc:contributor":["Stapleton, H.J."],"dc:creator":["Colvin, John Trevor"],"dc:date":["2011-06-07T15:02:29Z","10000-01-01","1984"],"dc:description":["The fractal model relating protein structure and vibrational dynamics is reviewed and refined. The temperature dependence of electron spin-lattice relaxation stimulated by Raman phonon scattering is measured in low spin ferric proteins. The data are analysed to yield the spectral dimension, a parameter characterizing the protein vibrational dynamics. Protein X-ray coordinate s are used to approximate a static structural parameter, the fractal dimension. These parameters are related as scaling exponents using simple physical arguments and experimental results. Central issues addressed are the domain of length scales over which the tabulated fractal dimension is a valid scaling exponent and the frequency range of protein vibrations contributing to the measurement of the spectral dimension. Recent experimental findings are interpreted to relate these regimes. They reveal a transition in the spectral dimension from reflecting the protein structure above 6K, to that of the surrounding solvent below this temperature.","Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-07T15:02:29Z No. of bitstreams: 1 1984_colvin.pdf: 3659139 bytes, checksum: 93bed8c1c0e9b1258f4e1b9ff5cf675a (MD5)","Made available in DSpace on 2011-06-07T15:02:29Z (GMT). No. of bitstreams: 1 1984_colvin.pdf: 3659139 bytes, checksum: 93bed8c1c0e9b1258f4e1b9ff5cf675a (MD5) Previous issue date: 1984","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-06-07T15:02:30Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:13:17-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis","Thesis","U of I Only"],"dc:identifier":["826562","http://hdl.handle.net/2142/25315"],"dc:language":["en"],"dc:rights":["1984 John Trevor Colvin"],"dc:subject":["electron spin-lattice relaxation","low spin iron proteins","protein structure","vibrational dynamics","Raman phonon scattering"],"dc:title":["Spin lattice relaxation studies on iron proteins"],"dc:type":["Dissertation / Thesis","text"],"thesis:degree_discipline":["Physics"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."]},"updated_at":"2026-07-22T22:25:24Z"}