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@ARTICLE{Kotov:435901,
      author       = {Kotov, Vadim and Bartels, Kim and Veith, Katharina and
                      Josts, Inokentijs and Subhramanyam, Udaya K. Tiruttani and
                      Günther, Christian and Labahn, Jörg and Marlovits, Thomas
                      C. and Moraes, Isabel and Tidow, Henning and Loew, Christian
                      and Garcia-Alai, Maria M.},
      title        = {{H}igh-throughput stability screening for
                      detergent-solubilized membrane proteins},
      journal      = {Scientific reports},
      volume       = {9},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {PUBDB-2020-00849},
      pages        = {10379},
      year         = {2019},
      abstract     = {Protein stability in detergent or membrane-like
                      environments is the bottleneck for structural studies on
                      integral membrane proteins (IMP). Irrespective of the method
                      to study the structure of an IMP, detergent solubilization
                      from the membrane is usually the first step in the workflow.
                      Here, we establish a simple, high-throughput screening
                      method to identify optimal detergent conditions for membrane
                      protein stabilization. We apply differential scanning
                      fluorimetry in combination with scattering upon thermal
                      denaturation to study the unfolding of integral membrane
                      proteins. Nine different prokaryotic and eukaryotic membrane
                      proteins were used as test cases to benchmark our detergent
                      screening method. Our results show that it is possible to
                      measure the stability and solubility of IMPs by diluting
                      them from their initial solubilization condition into
                      different detergents. We were able to identify groups of
                      detergents with characteristic stabilization and
                      destabilization effects for selected targets. We further
                      show that fos-choline and PEG family detergents may lead to
                      membrane protein destabilization and unfolding. Finally, we
                      determined thenmodynamic parameters that are important
                      indicators of IMP stability. The described protocol allows
                      the identification of conditions that are suitable for
                      downstream handling of membrane proteins during
                      purification.},
      cin          = {CSSB-UKE / CSSB-EMBL-CL / CSSB-UKE-TM / CSSB-FZJ-JL /
                      CSSB-CF-SPC},
      ddc          = {600},
      cid          = {I:(DE-H253)CSSB-UKE-20141216 /
                      I:(DE-H253)CSSB-EMBL-CL-20210806 /
                      I:(DE-H253)CSSB-UKE-TM-20210520 /
                      I:(DE-H253)CSSB-FZJ-JL-20210520 /
                      I:(DE-H253)CSSB-CF-SPC-20210520},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31316088},
      UT           = {WOS:000475832700023},
      doi          = {10.1038/s41598-019-46686-8},
      url          = {https://bib-pubdb1.desy.de/record/435901},
}