Ion mobility has emerged as an important technique for determining biopolymer conformations in solvent free environments. These experiments have been nearly exclusively performed on home built systems. In this paper we describe modifications to a commercial high performance mass spectrometer, the Waters UK "Uhima" Q-Tof, that allows high sensitivity measurement of peptide and protein cross sections. Arrival time distributions are obtained for a series of peptides (bradykinin, LHRH, substance P, bombesin) and proteins (bovine and equine cytochrome c, myoglobin, alpha-lactalbumin) with good agreement found with literature cross sections where available. In complex ATD's, mass spectra can be obtained for each feature confirming assignments. Th...
The characterization of biomolecules and biomolecular complexes represents an area of significant re...
The three-dimensional conformation of a protein is central to its biological function. The character...
High-field asymmetric waveform ion mobility spectrometry (FAIMS) enables the separation of ions on t...
One difficulty in using ion mobility (IM) mass spectrometry (MS) to improve the specificity of pepti...
Native mass spectrometry is a powerful tool for the analysis of noncovalent complexes. When coupled ...
Analysis and characterisation of biomolecules using mass spectrometry has advanced over the past dec...
Ion mobility mass spectrometry (IM-MS) allows separation of native protein ions into “conformational...
peer reviewedIon mobility (IM) mass spectrometry allows conducting data independent acquisition (DIA...
In the last thirty years, ion/ion reactions have been developed and applied to answer increasingly d...
Ion mobility mass spectrometry (IM-MS) allows separation of native protein ions into “conformational...
A commercially available ion mobility spectrometer was interfaced to a custom-built linear time-of-f...
Detailed knowledge of the tertiary and quaternary structure of proteins and protein complexes is of ...
In the present work, we employ trapped ion mobility spectrometry (TIMS) for conformational analysis ...
The field of ion mobility-mass spectrometry (IM-MS) has developed rapidly in recent decades, with ne...
Miniaturized ultra high field asymmetric waveform ion mobility spectrometry (ultra-FAIMS) combined w...
The characterization of biomolecules and biomolecular complexes represents an area of significant re...
The three-dimensional conformation of a protein is central to its biological function. The character...
High-field asymmetric waveform ion mobility spectrometry (FAIMS) enables the separation of ions on t...
One difficulty in using ion mobility (IM) mass spectrometry (MS) to improve the specificity of pepti...
Native mass spectrometry is a powerful tool for the analysis of noncovalent complexes. When coupled ...
Analysis and characterisation of biomolecules using mass spectrometry has advanced over the past dec...
Ion mobility mass spectrometry (IM-MS) allows separation of native protein ions into “conformational...
peer reviewedIon mobility (IM) mass spectrometry allows conducting data independent acquisition (DIA...
In the last thirty years, ion/ion reactions have been developed and applied to answer increasingly d...
Ion mobility mass spectrometry (IM-MS) allows separation of native protein ions into “conformational...
A commercially available ion mobility spectrometer was interfaced to a custom-built linear time-of-f...
Detailed knowledge of the tertiary and quaternary structure of proteins and protein complexes is of ...
In the present work, we employ trapped ion mobility spectrometry (TIMS) for conformational analysis ...
The field of ion mobility-mass spectrometry (IM-MS) has developed rapidly in recent decades, with ne...
Miniaturized ultra high field asymmetric waveform ion mobility spectrometry (ultra-FAIMS) combined w...
The characterization of biomolecules and biomolecular complexes represents an area of significant re...
The three-dimensional conformation of a protein is central to its biological function. The character...
High-field asymmetric waveform ion mobility spectrometry (FAIMS) enables the separation of ions on t...