Liquid chromatography (LC) coupled to a mass spectrometer (MS) makes it possible to separate and accurately measure the m/z of proteins or peptides. HPLC or nano columns aim to retain the molecules and individually release them again during a solvent gradient directly into the MS, where the samples get ionized and measured via their mass to charge ratio (m/z). The raw data can then be analysed by either a deconvolution software for intact protein masses or a database search against known protein sequences for peptide assignment.
Provide us, the research group Bioanalytics at the TU Vienna, with dry proteins, proteins in solution or even gel bands and we will prepare the samples according to the desired information for intact and/or sequencing analysis. Our experience in the technical equipment has already been proven many times in external projects. Most often we were able to resolve the proteins to their monoisotopic masses or reach 100% sequence coverages. With that we are able to check for impurities, all sorts of mutations, special modifications, protein sizes or degradation products.
Experts:Ruth Birner-Gruenberger, Ph.D.
Available for:Joint Research Project, Contract Research, Investments
Development status:Technology Readiness Level 6 (Demonstrated in relevant environment)
IPR:Can be generated for our industrial partners / investors
Keywords:LC-MS analysis, Protein sequence, Protein size, Point mutations, Protein stability, Protein purity, Protein modifications, Glycosylation
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