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Host-pathogen interactions:
mammalian-bacterial, honeybee-bacterial, honeybee-mite.
Our lab is focused on quantitative proteomics using LC-ESI-MS to study biological systems. We cover a wide range of topics including pathogen invasion, infection, protein localization, and mapping protein interaction.
Mass spectrometry-based proteomics:
In order to understand how a complex system works it is extremely useful to know the identities of as many of the components of the system as possible. Commercially available mass spectrometers and database search tools have advanced to the point where experienced laboratories can routinely and reliably identify hundreds or thousands of proteins in exceedingly complex mixtures (i.e. an organelle preparation) using nanoflow high performance liquid chromatography (HPLC)/tandem mass spectrometry (LC/MS). Typically, complex protein samples are reduced to peptides by highly specific enzymatic digestion (e.g. trypsin cleavage carboxy-terminal of Arg or Lys). The peptides are then resolved by extremely high-resolution reversed-phase chromatography and eluted/ionized directly into a mass spectrometer (MS). The MS, operating in an information-dependent mode, selects and isolates any peptide ions observed and subjects them to tandem mass spectrometry. The observed mass/charge ratio of the peptide and its fragmentation pattern are then used to scan comprehensive protein sequence libraries (e.g. for a human liver sample the data would be searched against the Homo sapiens library) to find the best theoretical match and the peptides are compiled to arrive at a ‘protein hit list’.
mammalian-bacterial, honeybee-bacterial, honeybee-mite.
Our lab is focused on quantitative proteomics using LC-ESI-MS to study biological systems. We cover a wide range of topics including pathogen invasion, infection, protein localization, and mapping protein interaction.
Mass spectrometry-based proteomics:
In order to understand how a complex system works it is extremely useful to know the identities of as many of the components of the system as possible. Commercially available mass spectrometers and database search tools have advanced to the point where experienced laboratories can routinely and reliably identify hundreds or thousands of proteins in exceedingly complex mixtures (i.e. an organelle preparation) using nanoflow high performance liquid chromatography (HPLC)/tandem mass spectrometry (LC/MS). Typically, complex protein samples are reduced to peptides by highly specific enzymatic digestion (e.g. trypsin cleavage carboxy-terminal of Arg or Lys). The peptides are then resolved by extremely high-resolution reversed-phase chromatography and eluted/ionized directly into a mass spectrometer (MS). The MS, operating in an information-dependent mode, selects and isolates any peptide ions observed and subjects them to tandem mass spectrometry. The observed mass/charge ratio of the peptide and its fragmentation pattern are then used to scan comprehensive protein sequence libraries (e.g. for a human liver sample the data would be searched against the Homo sapiens library) to find the best theoretical match and the peptides are compiled to arrive at a ‘protein hit list’.
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论文共 34 篇作者统计合作学者相似作者
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Brenna N. Hay, Mopelola O. Akinlaja, Teesha C. Baker,Aicha Asma Houfani,R. Greg Stacey,Leonard J. Foster
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