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Conformational studies of hairpin sequences from the ColE1 cruciform
dc.contributor.authorBlatt, N. B.en_US
dc.contributor.authorOsborne, Scott E.en_US
dc.contributor.authorCain, R. J.en_US
dc.contributor.authorGlick, Gary D.en_US
dc.date.accessioned2006-04-10T15:58:23Z
dc.date.available2006-04-10T15:58:23Z
dc.date.issued1993en_US
dc.identifier.citationBlatt, N. B., Osborne, S. E., Cain, R. J., Glick, G. D. (1993)."Conformational studies of hairpin sequences from the ColE1 cruciform." Biochimie 75(6): 433-441. <http://hdl.handle.net/2027.42/31086>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6VRJ-47S661V-6B/2/11aed1d325e3e5d1589096f146747491en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/31086
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8364093&dopt=citationen_US
dc.description.abstractInverted repeat sequences derived from the ColE1 cruciform were investigated by nuclear magnetic resonance (NMR) and UV spectroscopy. It was shown that 15 different sequences exist as stable hairpin structures over a range of buffer conditions and DNA concentrations. Experiments with six oligomers (1-6) containing the native stem sequence and five base loops, found that the two hairpins with the wild-type loops (1-2) served as upper and lower bounds for the thermodynamic stability of all the other sequences. NMR experiments, including rotational correlation time measurements and NOESY spectra, were then performed on 1, the most stable hairpin sequence to begin to uncover a structural basis of its stability.en_US
dc.format.extent1057314 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleConformational studies of hairpin sequences from the ColE1 cruciformen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USAen_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USAen_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USAen_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USAen_US
dc.identifier.pmid8364093en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/31086/1/0000763.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0300-9084(93)90108-5en_US
dc.identifier.sourceBiochimieen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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