{"id":{"repo_id":"mit","oai_identifier":"oai:dspace.mit.edu:1721.1/58201"},"canonical_url":"https://search.dev.ndltd.org/etd/mit/oai:dspace.mit.edu:1721.1/58201","repository":{"repo_id":"mit","name":"MIT","base_url":"https://dspace.mit.edu/oai/request"},"display":{"title":"Applications of DNP and solid-state NMR for protein structure determination","abstract":"Magic Angle Spinning (MAS) solid state nuclear magnetic resonance (SSNMR) is a developing method for determining the structures and studying the dynamics and functions of biological molecules. This method is particularly important for systems, such as amyloidogenic fibrous proteins, that do not crystallize or dissolve well and are therefore not amendable to X-ray or solution NMR techniques. However, due to inherently low sensitivity, NMR experiments may require weeks to obtain spectra with sufficient signal-to-noise ratio. This issue is further exacerbated for biological systems of interest due to their large size and limited mass availability. The sensitivity can be increased by two orders of magnitude by combining MAS NMR with dynamic nuclear polarization (DNP). The application of SSNMR-DNP to protein structure determination is explored using malonic acid and a model peptide system, WT-TTR105-115. A custom built MAS-SSNMR probe is modified for the purpose of MAS-SSNMR DNP experiments.","abstract_html":"Magic Angle Spinning (MAS) solid state nuclear magnetic resonance (SSNMR) is a developing method for determining the structures and studying the dynamics and functions of biological molecules. This method is particularly important for systems, such as amyloidogenic fibrous proteins, that do not crystallize or dissolve well and are therefore not amendable to X-ray or solution NMR techniques. However, due to inherently low sensitivity, NMR experiments may require weeks to obtain spectra with sufficient signal-to-noise ratio. This issue is further exacerbated for biological systems of interest due to their large size and limited mass availability. The sensitivity can be increased by two orders of magnitude by combining MAS NMR with dynamic nuclear polarization (DNP). The application of SSNMR-DNP to protein structure determination is explored using malonic acid and a model peptide system, WT-TTR105-115. A custom built MAS-SSNMR probe is modified for the purpose of MAS-SSNMR DNP experiments.","abstract_has_math":false,"creators":["Mayrhofer, Rebecca Maria"],"institution":"Massachusetts Institute of Technology","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":"Massachusetts Institute of Technology. Dept. of Chemistry.","school":null,"contributors":[],"advisors":["Robert G. Griffin."],"committee_chairs":[],"committee_members":[],"year":2010,"date_issued":"2010","date_published":"2010","updated_at":"2026-07-22T22:21:55Z","subjects":["Chemistry."],"languages":["eng"],"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."],"rights_urls":["http://dspace.mit.edu/handle/1721.1/7582"],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/1721.1/58201","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Robert G. Griffin."]},{"key":"dc:contributor.department","label":"Department","values":["Massachusetts Institute of Technology. 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Dept. of Chemistry."]},{"key":"dc:creator","label":"Author","values":["Mayrhofer, Rebecca Maria"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2010-09-02T15:01:55Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2010-09-02T15:01:55Z"]},{"key":"dc:date.issued","label":"Date","values":["2010"]},{"key":"dc:publisher","label":"Institution","values":["Massachusetts Institute of Technology"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry."]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["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."]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://dspace.mit.edu/handle/1721.1/7582"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/1721.1/58201"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2010.","Vita. Cataloged from PDF version of thesis.","Includes bibliographical references."]},{"key":"dc:description.abstract","label":"Abstract","values":["Magic Angle Spinning (MAS) solid state nuclear magnetic resonance (SSNMR) is a developing method for determining the structures and studying the dynamics and functions of biological molecules. This method is particularly important for systems, such as amyloidogenic fibrous proteins, that do not crystallize or dissolve well and are therefore not amendable to X-ray or solution NMR techniques. However, due to inherently low sensitivity, NMR experiments may require weeks to obtain spectra with sufficient signal-to-noise ratio. This issue is further exacerbated for biological systems of interest due to their large size and limited mass availability. The sensitivity can be increased by two orders of magnitude by combining MAS NMR with dynamic nuclear polarization (DNP). The application of SSNMR-DNP to protein structure determination is explored using malonic acid and a model peptide system, WT-TTR105-115. A custom built MAS-SSNMR probe is modified for the purpose of MAS-SSNMR DNP experiments."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["S.M."]},{"key":"dc:title","label":"Title","values":["Applications of DNP and solid-state NMR for protein structure determination"]}]}],"canonical_facts":{"dc:contributor.advisor":["Robert G. Griffin."],"dc:contributor.department":["Massachusetts Institute of Technology. Dept. of Chemistry."],"dc:contributor.other":["Massachusetts Institute of Technology. Dept. of Chemistry."],"dc:creator":["Mayrhofer, Rebecca Maria"],"dc:date.accessioned":["2010-09-02T15:01:55Z"],"dc:date.available":["2010-09-02T15:01:55Z"],"dc:date.issued":["2010"],"dc:description":["Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2010.","Vita. Cataloged from PDF version of thesis.","Includes bibliographical references."],"dc:description.abstract":["Magic Angle Spinning (MAS) solid state nuclear magnetic resonance (SSNMR) is a developing method for determining the structures and studying the dynamics and functions of biological molecules. This method is particularly important for systems, such as amyloidogenic fibrous proteins, that do not crystallize or dissolve well and are therefore not amendable to X-ray or solution NMR techniques. However, due to inherently low sensitivity, NMR experiments may require weeks to obtain spectra with sufficient signal-to-noise ratio. This issue is further exacerbated for biological systems of interest due to their large size and limited mass availability. The sensitivity can be increased by two orders of magnitude by combining MAS NMR with dynamic nuclear polarization (DNP). The application of SSNMR-DNP to protein structure determination is explored using malonic acid and a model peptide system, WT-TTR105-115. A custom built MAS-SSNMR probe is modified for the purpose of MAS-SSNMR DNP experiments."],"dc:description.degree":["S.M."],"dc:identifier.uri":["http://hdl.handle.net/1721.1/58201"],"dc:language.iso":["eng"],"dc:publisher":["Massachusetts Institute of Technology"],"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."],"dc:rights.uri":["http://dspace.mit.edu/handle/1721.1/7582"],"dc:subject":["Chemistry."],"dc:title":["Applications of DNP and solid-state NMR for protein structure determination"],"dc:type":["Thesis"]},"updated_at":"2026-07-22T22:21:55Z"}