Do you need to determine the glycosylation sites and status of your proteins? If so, PNGase F might be just what you need! PNGase F catalyses the cleavage of N-linked oligosaccharides between the innermost GlcNAc and asparagine residues of high mannose, hybrid and complex oligosaccharides from N-linked glycoproteins. Find out more at: https://bit.ly/3YTUbcn #MassSpectrometry #MassSpec
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Do you need to determine the glycosylation sites and status of your proteins? If so, PNGase F might be just what you need! PNGase F catalyses the cleavage of N-linked oligosaccharides between the innermost GlcNAc and asparagine residues of high mannose, hybrid and complex oligosaccharides from N-linked glycoproteins. #MassSpectrometry #MassSpec https://lnkd.in/e65238CS
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#callforreading #recommendations in Methods and Protocols MDPI Title: Inexpensive, Accurate, and Stable Method to Quantitate Blood Alanine Aminotransferase (ALT) Levels Authors: Phillipp Hartmann and Bernd Schnabl from University of California, San Francisco Read and Download for #free at: https://lnkd.in/g6_eDhHX #methods #protocol #blood #liverdisease #alanineaminotransferase #plasma #hemolysis #triglycerides
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C–H amination with pyrazole, triazole, and pyridine nucleophiles with A first-generation photocatalyst composed of Sc(OTf)3 and acridine.
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https://lnkd.in/ebzQWUty A chlorinative cyclization of aryl alkynoates in the presence of N-chlorosuccinimide (NCS) and Mes-Acr-MeClO4 as photocatalyst
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Salt bridges in proteins Salt bridges in proteins are bonds between oppositely charged residues that are sufficiently close to each other to experience electrostatic attraction. They contribute to protein structure and to the specificity of interaction of proteins with other biomolecules, but in doing so they need not necessarily increase a protein's free energy of unfolding. The salt bridge most often arises from the anionic carboxylate (RCOO ) of either aspartic acid or glutamic acid and the cationic ammonium (RNH3+) from lysine or the guanidinium (RNHC(NH2)2+) of arginine. Salt bridges: A) Form when oppositely-charged amino acid side chains contact each other B) Form when positively charged amino acid side chains contact each other C) Form mostly in the core of the molecule D) Form mostly on the surface of the molecule E) Are covalent bonds Youtube video: https://lnkd.in/dC5fQMp7 #nikolaysgeneticslessons
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The CH₂ group of the acetamide moiety represents an attractive attachment point for additional exit vectors. Involving this carbon in the piperidine ring greatly increase the compound’s potency on LPAR1 and improv its metabolic stability (https://lnkd.in/gWJ-kK3D). Try our piperidine building blocks in your research! https://lnkd.in/dcruJs4V
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https://lnkd.in/evDN2UmA A chlorinative cyclization of aryl alkynoates in the presence of N-chlorosuccinimide (NCS) and Mes-Acr-MeClO4 as photocatalyst
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A Green and Efficient Approach for Preparation of Diaryl Sulfones: Fe3O4@DABA-PA-CuBr2 Nanocomposite Catalyzed One-Pot Three-Component Aryl Iodides, Aryl Boronic Acids, and DABSO (as SO2 Source)
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