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Mass spectrometry of membrane protein complexes.
Bender, Julian; Schmidt, Carla.
Afiliación
  • Bender J; Interdisciplinary Research Center HALOmem, Charles Tanford Protein Centre, Martin Luther University Halle-Wittenberg, Institute for Biochemistry and Biotechnology, Kurt-Mothes-Str. 3a, D-06120 Halle, Germany.
  • Schmidt C; Interdisciplinary Research Center HALOmem, Charles Tanford Protein Centre, Martin Luther University Halle-Wittenberg, Institute for Biochemistry and Biotechnology, Kurt-Mothes-Str. 3a, D-06120 Halle, Germany.
Biol Chem ; 400(7): 813-829, 2019 06 26.
Article en En | MEDLINE | ID: mdl-30956223
ABSTRACT
Membrane proteins are key players in the cell. Due to their hydrophobic nature they require solubilising agents such as detergents or membrane mimetics during purification and, consequently, are challenging targets in structural biology. In addition, their natural lipid environment is crucial for their structure and function further hampering their analysis. Alternative approaches are therefore required when the analysis by conventional techniques proves difficult. In this review, we highlight the broad application of mass spectrometry (MS) for the characterisation of membrane proteins and their interactions with lipids. We show that MS unambiguously identifies the protein and lipid components of membrane protein complexes, unravels their three-dimensional arrangements and further provides clues of protein-lipid interactions.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Espectrometría de Masas / Proteínas de la Membrana Idioma: En Revista: Biol Chem Asunto de la revista: BIOQUIMICA Año: 2019 Tipo del documento: Article País de afiliación: Alemania

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Espectrometría de Masas / Proteínas de la Membrana Idioma: En Revista: Biol Chem Asunto de la revista: BIOQUIMICA Año: 2019 Tipo del documento: Article País de afiliación: Alemania