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dc.contributor.authorDunlop, Alex
dc.contributor.authorBowman, Kate
dc.contributor.authorAarstad, Olav Andreas
dc.contributor.authorSkjåk-Bræk, Gudmund
dc.contributor.authorStokke, Bjørn Torger
dc.contributor.authorRound, Andrew N
dc.date.accessioned2018-04-20T09:25:12Z
dc.date.available2018-04-20T09:25:12Z
dc.date.created2017-08-22T16:36:03Z
dc.date.issued2017
dc.identifier.citationNanoscale. 2017, 9 (39), 15089-15097.nb_NO
dc.identifier.issn2040-3364
dc.identifier.urihttp://hdl.handle.net/11250/2495251
dc.description.abstractWe evaluate an AFM-based single molecule force spectroscopy method for mapping sequences in otherwise difficult to sequence heteropolymers, including glycosylated proteins and glycans. The sliding contact force spectroscopy (SCFS) method exploits a sliding contact made between a nanopore threaded over a polymer axle and an AFM probe. We find that for sliding α- and β-cyclodextrin nanopores over a wide range of hydrophilic monomers, the free energy of sliding is proportional to the sum of two dimensionless, easily calculable parameters representing the relative partitioning of the monomer inside the nanopore or in the aqueous phase, and the friction arising from sliding the nanopore over the monomer. Using this relationship we calculate sliding energies for nucleic acids, amino acids, glycan and synthetic monomers and predict on the basis of these calculations that SCFS will detect N- and O-glycosylation of proteins and patterns of sidechains in glycans. For these applications, SCFS offers an alternative to sequence mapping by mass spectrometry or newly-emerging nanopore technologies that may be easily implemented using a standard AFM.nb_NO
dc.language.isoengnb_NO
dc.publisherRoyal Society of Chemistrynb_NO
dc.titlePolymer sequencing by molecular machines: a framework for predicting the resolving power of a sliding contact force spectroscopy sequencing methodnb_NO
dc.typeJournal articlenb_NO
dc.description.versionsubmittedVersionnb_NO
dc.source.pagenumber15089-15097nb_NO
dc.source.volume9nb_NO
dc.source.journalNanoscalenb_NO
dc.source.issue39nb_NO
dc.identifier.doi10.1039/c7nr03358c
dc.identifier.cristin1487966
dc.relation.projectNorges forskningsråd: 221576nb_NO
dc.description.localcodeThis is a submitted manuscript of an article published by Royal Society of Chemistry in Nanoscale, 02 Oct 2017nb_NO
cristin.unitcode194,66,15,0
cristin.unitcode194,66,20,0
cristin.unitnameInstitutt for bioteknologi og matvitenskap
cristin.unitnameInstitutt for fysikk
cristin.ispublishedtrue
cristin.fulltextpostprint
cristin.qualitycode1


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