Detection of endogenous ubiquitination sites by mass spectrometry has dramatically improved with the commercialization of anti-di-glycine remnant (K-ε-GG) antibodies. Here, we describe a number of improvements to the K-ε-GG enrichment workflow, including optimized antibody and peptide input requirements, antibody cross-linking
Journal of the American Society for Mass Spectrometry, 23(4), 621-631 (2011-09-29)
We present a full computational description of the fragmentation reactions of protonated diglycine (H(+)GG). Relaxed potential energy surface scans performed at B3LYP/6-31 G(d) or B3LYP/6-311 + G(d,p) levels are used to map the reaction coordinate surfaces and identify the transition states (TSs) and
Journal of the American Society for Mass Spectrometry, 23(4), 632-643 (2011-09-29)
We present a full molecular description of fragmentation reactions of protonated diglycine (H(+)GG) by studying their collision-induced dissociation (CID) with Xe using a guided ion beam tandem mass spectrometer (GIBMS). Analysis of the kinetic energy-dependent CID cross sections provides the
The rhomboid family of serine proteases occurs in all domains of life. Its members contain at least six hydrophobic membrane-spanning helices, with an active site serine located deep within the hydrophobic interior of the plasma membrane. The model member GlpG
Posttranslational modifications of proteins increase the complexity of the cellular proteome and enable rapid regulation of protein functions in response to environmental changes. Protein ubiquitylation is a central regulatory posttranslational modification that controls numerous biological processes including proteasomal degradation of
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