Optimization of protein samples for NMR using thermal shift assays

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dc.identifier.uri http://dx.doi.org/10.15488/1027
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/1051
dc.contributor.author Kozak, Sandra
dc.contributor.author Lercher, Lukas
dc.contributor.author Karanth, Megha N.
dc.contributor.author Meijers, Rob
dc.contributor.author Carlomagno, Teresa
dc.contributor.author Boivin, Stephane
dc.date.accessioned 2017-01-12T08:35:29Z
dc.date.available 2017-01-12T08:35:29Z
dc.date.issued 2016
dc.identifier.citation Kozak, S.; Lercher, L.; Karanth, M.N.; Meijers, R.; Carlomagno, T. et al.: Optimization of protein samples for NMR using thermal shift assays. In: Journal of Biomolecular NMR 64 (2016), Nr. 4, S. 281-289. DOI: http://dx.doi.org/10.1007/s10858-016-0027-z
dc.description.abstract Maintaining a stable fold for recombinant proteins is challenging, especially when working with highly purified and concentrated samples at temperatures >20 °C. Therefore, it is worthwhile to screen for different buffer components that can stabilize protein samples. Thermal shift assays or ThermoFluor® provide a high-throughput screening method to assess the thermal stability of a sample under several conditions simultaneously. Here, we describe a thermal shift assay that is designed to optimize conditions for nuclear magnetic resonance studies, which typically require stable samples at high concentration and ambient (or higher) temperature. We demonstrate that for two challenging proteins, the multicomponent screen helped to identify ingredients that increased protein stability, leading to clear improvements in the quality of the spectra. Thermal shift assays provide an economic and time-efficient method to find optimal conditions for NMR structural studies. © 2016, The Author(s). eng
dc.description.sponsorship EU/FP7/2007–2013
dc.description.sponsorship European Molecular Biology Laboratory
dc.description.sponsorship EMBO Long-term Fellowship
dc.language.iso eng
dc.publisher Dordrecht : Springer Netherlands
dc.relation.ispartofseries Journal of Biomolecular NMR 64 (2016), Nr. 4
dc.rights CC BY 4.0
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject Differential scanning fluorimetry eng
dc.subject Nuclear magnetic resonance eng
dc.subject Protein thermal stability eng
dc.subject Sample optimization eng
dc.subject Thermal shift assay eng
dc.subject ThermoFluor eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.title Optimization of protein samples for NMR using thermal shift assays
dc.type Text
dc.type article
dc.relation.essn 1573-5001
dc.relation.issn 0925-2738
dc.relation.doi https://doi.org/10.1007/s10858-016-0027-z
dc.bibliographicCitation.issue 4
dc.bibliographicCitation.volume 64
dc.bibliographicCitation.firstPage 281
dc.bibliographicCitation.lastPage 289
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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