In ESI, with a single pure proteofrom being ionised, each peak will represent a different charge state of the protein, with a smaller m/z being a higher charge state (more H+ attached). To work out the mass of the protein, simultaneous equations can be used and this can be done manually with enough time. Software that comes with the MS often does this, but there is also online calculators like this one: www.bioprocess.org/esiprot/esiprot_form.php.
Bwahahahahahahaha! No, I'm not a smoker. But the audio was recorded at about 7am in my office by myself with a headset. I realise that I need to be more dynamic.
Hello Dr. I will like to know if you have a published paper concerning this overview because I will like to use it as one of my references for a research paper I'm writing on "Translational Proteomics with Advanced Mass Spectrometry (MS) Systems".
This is all out of my own head using articles and text books that were already out there, along with discussions with engineers. So I don't have a single article. If you email me, I'll try and find some srticles to send you.
Four years and someone finally picks up a 'mistake'. You tell me what the common name for an uncharged ion is, one that is able to enter the MS, be past through the instrument and able to strike the detector, giving a false signal? An uncharged molecule, I guess.
This is a great summary but there are some serious copyright infringement issues with this video. The simulations in the LC-MS are straight from Thermo Scientific. There is no credit attributed to Thermo anywhere in the video and it is not clear that permission has been given for use of their video.
