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Showing 1 to 4 of 4 for “"Collision induced unfolding."”.

  1. Comparing Solution-Phase and Gas-Phase Protein Stability Using Ion Mobility and Differential Mobility Mass Spectrometry

    … of a protein using a fluorescent dye to monitor unfolding. Protein unfolding has also been studies with mass spectrometry through collision induced unfolding (CIU) whereby the ion temperature in the trap collision cell is increased and unfolding changes are tracked in the ion mobility cell. …

    york Repository record for Comparing Solution-Phase and Gas-Phase Protein Stability Using Ion Mobility and Differential Mobility Mass Spectrometry (opens in a new tab)

  2. Characterizing Conformational Dynamics and Catalytic Activity of Enzymes by Hydrogen-Deuterium Exchange Mass Spectrometry

    … all protein/substrate complexes. Additionally, collision induced unfolding (CIU) within the ion mobility cell provides a comparative binding affinity scale for the inhibitory drugs used in the study of TEM-1. Using this wide range of analytical techniques facilitated important discoveries …

    york Repository record for Characterizing Conformational Dynamics and Catalytic Activity of Enzymes by Hydrogen-Deuterium Exchange Mass Spectrometry (opens in a new tab)

  3. Native surface mass spectrometry via static liquid extraction and laser ablation sampling for structural characterization of macromolecules in gas phase.

    … under native surface MS conditions. Multiplexed collision induced unfolding (CIU) results from ion mobility mass spectrometry (IM-MS) data showed that unfolding pathway dynamics for proteins sampled via solid-liquid microextraction and laser ablation capture were analogous. Although the presence …

    baylor Repository record for Native surface mass spectrometry via static liquid extraction and laser ablation sampling for structural characterization of macromolecules in gas phase. (opens in a new tab)

  4. Investigating structural and stability characteristics of native-like proteins using ion mobility-mass spectrometry (IM-MS) in positive- and negative-ion mode.

    Native ion mobility-mass spectrometry (IMS-MS) is widely used to investigate the structure and stability of biologically relevant proteins and protein complexes. The key goal, and arguably biggest attraction, of native IMS-MS is maintaining the noncovalent interactions responsible for stabilizing …

    baylor Repository record for Investigating structural and stability characteristics of native-like proteins using ion mobility-mass spectrometry (IM-MS) in positive- and negative-ion mode. (opens in a new tab)