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dc.contributor.advisorVasskog, Terje
dc.contributor.authorMoen, Merete Kveli
dc.date.accessioned2015-03-11T06:11:16Z
dc.date.accessioned2016-05-20T12:20:12Z
dc.date.available2016-05-20T12:20:12Z
dc.date.issued2014-05-20
dc.description.abstractConotoxins are diverse and well-studied, and is therefore suited as a model to develop a general method for analyzing disulfide-rich peptides. To investigate the folding of both commercially available and self-synthesized Conotoxins, an UHPLC-MS/MS method was developed where one disulfide-bridge was reduced at the time and alkylated with different maleimides. The results from the UHPLC-MS/MS method were examined in a peptide- and protein-structure determination software.en_US
dc.identifier.urihttps://hdl.handle.net/10037/9226
dc.identifier.urnURN:NBN:no-uit_munin_8784
dc.language.isoengen_US
dc.publisherUiT Norges arktiske universiteten_US
dc.publisherUiT The Arctic University of Norwayen_US
dc.rights.accessRightsopenAccess
dc.rights.holderCopyright 2014 The Author(s)
dc.rights.urihttps://creativecommons.org/licenses/by-nc-sa/3.0en_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 Unported (CC BY-NC-SA 3.0)en_US
dc.subject.courseIDFAR-3901en_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Kjemi: 440::Analytisk kjemi: 445en_US
dc.subjectVDP::Mathematics and natural science: 400::Chemistry: 440::Analytical chemistry: 445en_US
dc.titleDetermination of Cysteine Connectivity in Bioactive Peptidesen_US
dc.typeMaster thesisen_US
dc.typeMastergradsoppgaveen_US


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Attribution-NonCommercial-ShareAlike 3.0 Unported (CC BY-NC-SA 3.0)
Med mindre det står noe annet, er denne innførselens lisens beskrevet som Attribution-NonCommercial-ShareAlike 3.0 Unported (CC BY-NC-SA 3.0)