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Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction.
Kaldmäe, Margit; Österlund, Nicklas; Lianoudaki, Danai; Sahin, Cagla; Bergman, Peter; Nyman, Tomas; Kronqvist, Nina; Ilag, Leopold L; Allison, Timothy M; Marklund, Erik G; Landreh, Michael.
Afiliación
  • Kaldmäe M; Science for Life Laboratory, Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 171 65, Stockholm, Sweden.
  • Österlund N; Department of Biochemistry and Biophysics, Stockholm University, 106 91, Stockholm, Sweden.
  • Lianoudaki D; Department of Environmental Science and Analytical Chemistry, Stockholm University, 106 91, Stockholm, Sweden.
  • Sahin C; Science for Life Laboratory, Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 171 65, Stockholm, Sweden.
  • Bergman P; Science for Life Laboratory, Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 171 65, Stockholm, Sweden.
  • Nyman T; Division of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institutet, 141 86, Huddinge, Sweden.
  • Kronqvist N; Protein Science Facility, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, 171 65, Stockholm, Sweden.
  • Ilag LL; Division for Neurogeriatrics, Department of Neurobiology, Care Sciences and Society (NVS), Karolinska Institutet, 141 83, Huddinge, Sweden.
  • Allison TM; Department of Environmental Science and Analytical Chemistry, Stockholm University, 106 91, Stockholm, Sweden.
  • Marklund EG; Biomolecular Interaction Centre and School of Physical and Chemical Sciences, University of Canterbury, Christchurch, 8140, New Zealand.
  • Landreh M; Department of Chemistry - BMC, Uppsala University, Box 576, 751 23, Uppsala, Sweden.
J Am Soc Mass Spectrom ; 30(8): 1385-1388, 2019 Aug.
Article en En | MEDLINE | ID: mdl-31286443
Modulating protein ion charge is a useful tool for the study of protein folding and interactions by electrospray ionization mass spectrometry. Here, we investigate activation-dependent charge reduction of protein ions with the chemical chaperone trimethylamine-N-oxide (TMAO). Based on experiments carried out on proteins ranging from 4.5 to 35 kDa, we find that when combined with collisional activation, TMAO removes approximately 60% of the charges acquired under native conditions. Ion mobility measurements furthermore show that TMAO-mediated charge reduction produces the same end charge state and arrival time distributions for native-like and denatured protein ions. Our results suggest that gas-phase collisions between the protein ions and TMAO result in proton transfer, in line with previous findings for dimethyl- and trimethylamine. By adjusting the energy of the collisions experienced by the ions, it is possible to control the degree of charge reduction, making TMAO a highly dynamic charge reducer that opens new avenues for manipulating protein charge states in ESI-MS and for investigating the relationship between protein charge and conformation. ᅟ.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas / Espectrometría de Masa por Ionización de Electrospray / Metilaminas Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: J Am Soc Mass Spectrom Año: 2019 Tipo del documento: Article País de afiliación: Suecia Pais de publicación: Estados Unidos
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas / Espectrometría de Masa por Ionización de Electrospray / Metilaminas Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: J Am Soc Mass Spectrom Año: 2019 Tipo del documento: Article País de afiliación: Suecia Pais de publicación: Estados Unidos