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Modified Ion Source for the Improved Collisional Activation of Protein Complexes.
Schrader, Robert L; Walker, Thomas E; Russell, David H.
Afiliación
  • Schrader RL; Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States.
  • Walker TE; Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States.
  • Russell DH; Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States.
J Am Soc Mass Spectrom ; 34(5): 977-980, 2023 May 03.
Article en En | MEDLINE | ID: mdl-37001029
The analysis of large molecules is challenging, as they often have salts and adducts retained through the electrospray process, which increase the observed mass and compromise the achievable mass resolution. Mild collisional activation has been shown to be very effective for the removal of adducts and increases both measurement accuracy and mass resolution of large (>100 kDa) protein complexes. Collisionally activated protein ions are more completely desolvated due to the increased number of collisions when trapped following activation. A short square quadrupole maintained at 300 mTorr by a mechanical pump was added between the ion funnel and transmission quadrupole. This configuration and operation effectively removed adducts from the 800 kDa tetradecamer GroEL as well as fragmented smaller protein complexes like C-reactive protein. Due to the gas high pressure, ions of low size-to-charge ratio, such as those in charge reducing buffers, had low ejection efficiency. We show that segmenting the quadrupole rods greatly improves signal intensity for charge reduced GroEL D398A mutant compared to nonsegmented rods when operating at high pressure.
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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Espectrometría de Masas Idioma: En Revista: J Am Soc Mass Spectrom Año: 2023 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Espectrometría de Masas Idioma: En Revista: J Am Soc Mass Spectrom Año: 2023 Tipo del documento: Article