Journal Article FZJ-2017-08171

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Invisible detergents for structure determination of membrane proteins by small-angle neutron scattering

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2018
Wiley-Blackwell Oxford [u.a.]

The FEBS journal 285(2), 357–371 () [10.1111/febs.14345]

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Abstract: A novel and generally applicable method for determining structures of membrane proteins in solution via small-angle neutron scattering (SANS) is presented. Common detergents for solubilizing membrane proteins were synthesized in isotope-substituted versions for utilizing the intrinsic neutron scattering length difference between hydrogen and deuterium. Individual hydrogen/deuterium levels of the detergent head and tail groups were achieved such that the formed micelles became effectively invisible in heavy water (D2O) when investigated by neutrons. This way, only the signal from the membrane protein remained in the SANS data. We demonstrate that the method is not only generally applicable on five very different membrane proteins but also reveals subtle structural details about the sarco/endoplasmatic reticulum Ca2+ ATPase (SERCA). In all, the synthesis of isotope-substituted detergents makes solution structure determination of membrane proteins bySANS and subsequent data analysis available to non-specialists.

Keyword(s): Health and Life (1st) ; Biology (2nd) ; Soft Condensed Matter (2nd)

Classification:

Contributing Institute(s):
  1. JCNS-FRM-II (JCNS-FRM-II)
  2. Neutronenstreuung (Neutronenstreuung ; JCNS-1)
Research Program(s):
  1. 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623) (POF3-623)
  2. 6G15 - FRM II / MLZ (POF3-6G15) (POF3-6G15)
Experiment(s):
  1. KWS-1: Small angle scattering diffractometer (NL3b)

Appears in the scientific report 2018
Database coverage:
Medline ; OpenAccess ; BIOSIS Previews ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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Institute Collections > JCNS > JCNS-FRM-II
Document types > Articles > Journal Article
Institute Collections > JCNS > JCNS-1
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Open Access

 Record created 2017-12-11, last modified 2021-01-29