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dc.contributor.authorLewis, Karen A. ( Orcid Icon 0000-0001-9495-3977 )
dc.contributor.authorAltschuler, Sarah E. ( )
dc.contributor.authorWuttke, Deborah ( Orcid Icon 0000-0002-8158-8795 )
dc.date.accessioned2020-03-13T18:10:48Z
dc.date.available2020-03-13T18:10:48Z
dc.date.issued2019
dc.identifier.citationLewis, K. A., Altschuler, S. E., & Wuttke, D. S. (2019). Measuring low-picomolar apparent binding affinities by minigel electrophoretic mobility shift. Methods in Molecular Biology, 1855.en_US
dc.identifier.issn1940-6029
dc.identifier.urihttps://digital.library.txstate.edu/handle/10877/9447
dc.description.abstractMeasuring protein/DNA interactions that have apparent binding affinity constants in the low-picomolar range presents a unique experimental challenge. To probe the sequence specificity of telomere binding proteins, our laboratory has developed an electrophoretic mobility shift assay protocol that allows for the routine measurement of K D,app values in the 1-20 pM range. Here, we describe the protocol and highlight the particular considerations that should be made to successfully and reproducibly measure high-affinity interactions between proteins and single-stranded DNA.en_US
dc.formatText
dc.format.extent12 pages
dc.format.medium1 file (.pdf)
dc.language.isoen_USen_US
dc.publisherHumana Pressen_US
dc.sourceMethods in Molecular Biology, 2019, Vol. 1855.
dc.subjectNative gelen_US
dc.subjectEMSA
dc.subjectDNA binding protein
dc.subjectBinding assay
dc.subjectHigh-affinity binding
dc.titleMeasuring Low-Picomolar Apparent Binding Affinities by Minigel Electrophoretic Mobility Shiften_US
txstate.documenttypeArticle
dc.identifier.doihttps://doi.org/10.1007/978-1-4939-8793-1_29
dc.rights.licenseThis is the accepted manuscript version of an article published in Methods in Molecular Biology.
txstate.departmentChemistry and Biochemistry


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