{"id":{"repo_id":"aachen","oai_identifier":"oai:publications.rwth-aachen.de:52346"},"canonical_url":"https://search.dev.ndltd.org/etd/aachen/oai:publications.rwth-aachen.de:52346","repository":{"repo_id":"aachen","name":"RWTH Aachen University","base_url":"https://publications.rwth-aachen.de/oai2d"},"display":{"title":"Funktionsbasierte Isolierung von Subproteomen mit trifunktionellen Fangverbindungen","abstract":"Isolation, identification and quantitation of functional subproteomes by use of trifunctional capture compounds™, followed by mass spectrometric analysis, is a relatively new, promising technology for proteomic research. Particularly for analysis of effects and side effects of drugs or plant protection agents, as well as for the molecular biological basic research, the capability of this technology could be immense. When in 2005 the first photoaktivable capture compound™ for methyltransferases was avaiable at Aachen University, it was still unclear how it should be implemented to obtain samples suitable to further mass spectrometric analysis. An important challenge during this work was therefore, working out suitable basic conditions. This included the checkout of a suitable pretreatment of test material, viable buffer terms and efficient photo activation, as well as the maximization of the yield in specific proteins and a minimization of non-specific proteins. As a second aim, the new technology should be tested with the model organism E. coli. This, at the one hand, was a good demonstration of her applicability and, at the other hand, posed a challenge in that many of the target proteins thitherto have never been isolated. Beyond that, these rare expressed target proteins do not show a high affinity towards their cofactor and the used capture compound™. E. colis “methylome” therefore was a fascinating test object to check out the new methods capabilities and enabled a fair comparison to other up to date techniques.","abstract_html":"Isolation, identification and quantitation of functional subproteomes by use of trifunctional capture compounds™, followed by mass spectrometric analysis, is a relatively new, promising technology for proteomic research. Particularly for analysis of effects and side effects of drugs or plant protection agents, as well as for the molecular biological basic research, the capability of this technology could be immense. When in 2005 the first photoaktivable capture compound™ for methyltransferases was avaiable at Aachen University, it was still unclear how it should be implemented to obtain samples suitable to further mass spectrometric analysis. An important challenge during this work was therefore, working out suitable basic conditions. This included the checkout of a suitable pretreatment of test material, viable buffer terms and efficient photo activation, as well as the maximization of the yield in specific proteins and a minimization of non-specific proteins. As a second aim, the new technology should be tested with the model organism E. coli. This, at the one hand, was a good demonstration of her applicability and, at the other hand, posed a challenge in that many of the target proteins thitherto have never been isolated. Beyond that, these rare expressed target proteins do not show a high affinity towards their cofactor and the used capture compound™. E. colis “methylome” therefore was a fascinating test object to check out the new methods capabilities and enabled a fair comparison to other up to date techniques.","abstract_has_math":false,"creators":["Poot, Peter"],"institution":"Publikationsserver der RWTH Aachen University","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Weinhold, Elmar"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011","date_published":"2011","updated_at":"2026-07-30T19:40:50Z","subjects":["info:eu-repo/classification/ddc/570","Transferasen","Methyltransferasen","Adenosylmethionin","Proteomanalyse","LC-MS","Proteine","DNS-Methyltransferase","Escherichia coli","Biowissenschaften, Biologie","Methyltransferase","Fangverbindung","SAM","SAH","proteomics","capture compound","AdoMet","AdoHcy"],"languages":["ger"],"rights":["info:eu-repo/semantics/openAccess"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114577%22"],"render_values":[{"text":"https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114577%22","href":"https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114577%22","code":true}]}]},"links":{"outbound_url":"https://publications.rwth-aachen.de/record/52346","outbound_label":"Repository record","outbound_source":"dc:identifier"},"source_record":{"url":"https://publications.rwth-aachen.de/oai2d?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai%3Apublications.rwth-aachen.de%3A52346","prefix":"oai_dc"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Weinhold, Elmar"]},{"key":"dc:creator","label":"Author","values":["Poot, Peter"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:coverage","label":"Dc Coverage","values":["DE"]},{"key":"dc:date","label":"Dc Date","values":["2011"]},{"key":"dc:publisher","label":"Institution","values":["Publikationsserver der RWTH Aachen University"]},{"key":"dc:relation","label":"Dc Relation","values":["info:eu-repo/semantics/altIdentifier/urn/urn:nbn:de:hbz:82-opus-39111"]},{"key":"dc:type","label":"Dc Type","values":["info:eu-repo/semantics/doctoralThesis","info:eu-repo/semantics/publishedVersion"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["info:eu-repo/classification/ddc/570","Transferasen","Methyltransferasen","Adenosylmethionin","Proteomanalyse","LC-MS","Proteine","DNS-Methyltransferase","Escherichia coli","Biowissenschaften, Biologie","Methyltransferase","Fangverbindung","SAM","SAH","proteomics","capture compound","AdoMet","AdoHcy"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["ger"]},{"key":"dc:rights","label":"Dc Rights","values":["info:eu-repo/semantics/openAccess"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://publications.rwth-aachen.de/record/52346","https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114577%22"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Isolation, identification and quantitation of functional subproteomes by use of trifunctional capture compounds™, followed by mass spectrometric analysis, is a relatively new, promising technology for proteomic research. Particularly for analysis of effects and side effects of drugs or plant protection agents, as well as for the molecular biological basic research, the capability of this technology could be immense. When in 2005 the first photoaktivable capture compound™ for methyltransferases was avaiable at Aachen University, it was still unclear how it should be implemented to obtain samples suitable to further mass spectrometric analysis. An important challenge during this work was therefore, working out suitable basic conditions. This included the checkout of a suitable pretreatment of test material, viable buffer terms and efficient photo activation, as well as the maximization of the yield in specific proteins and a minimization of non-specific proteins. As a second aim, the new technology should be tested with the model organism E. coli. This, at the one hand, was a good demonstration of her applicability and, at the other hand, posed a challenge in that many of the target proteins thitherto have never been isolated. Beyond that, these rare expressed target proteins do not show a high affinity towards their cofactor and the used capture compound™. E. colis “methylome” therefore was a fascinating test object to check out the new methods capabilities and enabled a fair comparison to other up to date techniques."]},{"key":"dc:source","label":"Dc Source","values":["Aachen : Publikationsserver der RWTH Aachen University IX, 196 S. : Ill., graph. Darst. (2011). = Aachen, Techn. Hochsch., Diss., 2011"]},{"key":"dc:title","label":"Title","values":["Funktionsbasierte Isolierung von Subproteomen mit trifunktionellen Fangverbindungen"]}]}],"canonical_facts":{"dc:contributor":["Weinhold, Elmar"],"dc:coverage":["DE"],"dc:creator":["Poot, Peter"],"dc:date":["2011"],"dc:description":["Isolation, identification and quantitation of functional subproteomes by use of trifunctional capture compounds™, followed by mass spectrometric analysis, is a relatively new, promising technology for proteomic research. Particularly for analysis of effects and side effects of drugs or plant protection agents, as well as for the molecular biological basic research, the capability of this technology could be immense. When in 2005 the first photoaktivable capture compound™ for methyltransferases was avaiable at Aachen University, it was still unclear how it should be implemented to obtain samples suitable to further mass spectrometric analysis. An important challenge during this work was therefore, working out suitable basic conditions. This included the checkout of a suitable pretreatment of test material, viable buffer terms and efficient photo activation, as well as the maximization of the yield in specific proteins and a minimization of non-specific proteins. As a second aim, the new technology should be tested with the model organism E. coli. This, at the one hand, was a good demonstration of her applicability and, at the other hand, posed a challenge in that many of the target proteins thitherto have never been isolated. Beyond that, these rare expressed target proteins do not show a high affinity towards their cofactor and the used capture compound™. E. colis “methylome” therefore was a fascinating test object to check out the new methods capabilities and enabled a fair comparison to other up to date techniques."],"dc:identifier":["https://publications.rwth-aachen.de/record/52346","https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114577%22"],"dc:language":["ger"],"dc:publisher":["Publikationsserver der RWTH Aachen University"],"dc:relation":["info:eu-repo/semantics/altIdentifier/urn/urn:nbn:de:hbz:82-opus-39111"],"dc:rights":["info:eu-repo/semantics/openAccess"],"dc:source":["Aachen : Publikationsserver der RWTH Aachen University IX, 196 S. : Ill., graph. Darst. (2011). = Aachen, Techn. Hochsch., Diss., 2011"],"dc:subject":["info:eu-repo/classification/ddc/570","Transferasen","Methyltransferasen","Adenosylmethionin","Proteomanalyse","LC-MS","Proteine","DNS-Methyltransferase","Escherichia coli","Biowissenschaften, Biologie","Methyltransferase","Fangverbindung","SAM","SAH","proteomics","capture compound","AdoMet","AdoHcy"],"dc:title":["Funktionsbasierte Isolierung von Subproteomen mit trifunktionellen Fangverbindungen"],"dc:type":["info:eu-repo/semantics/doctoralThesis","info:eu-repo/semantics/publishedVersion"]},"updated_at":"2026-07-30T19:40:50Z"}