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1 te of S. aureus sortase SrtA is specific for diglycine.
2 ated and identified by LC-ESI-MS as catechol-diglycine adduct that undergoes polymerization with othe
3 cine adopt zwitterionic structures, sodiated diglycine adopts a salt-bridge form, and sodiated trigly
4 tides containing lysine residues modified by diglycine, an adduct left at sites of ubiquitination aft
5 of a sulfonated tryptic peptide containing a diglycine branch generates a unique spectrum composed of
6 s of one glycine residue from the sulfonated diglycine branch) that can directly reveal the amino aci
7 on of ubiquitin-conjugated proteins produces diglycine branched peptides containing the modification
9 on of ubiquitin conjugated proteins produces diglycine branched peptides in which the C-terminal Gly-
10 ner, but several fragments characteristic to diglycine branched peptides were observed under low coll
13 olvation) free energies of (Gly)n and cyclic diglycine (cGG) and analyze the data according to experi
14 ilized a monoclonal antibody that recognizes diglycine (diGly)-containing isopeptides following tryps
16 the polyglycine acceptor nucleophile beyond diglycine does not further enhance the binding and catal
19 gous label that is chemically similar to the diglycine (GlyGly) tag, which is left at the ubiquitinat
20 elix, which alters bending and rotation at a diglycine hinge connecting the dimerization and cleavage
21 g two identical fragments head-to-tail using diglycine increases the proportion of cylindrin-sized ol
22 ipitation using an antibody specific for the diglycine-labeled internal lysine residue indicative of
24 chelate on biodistribution, mercapto-acetyl diglycine (MAG(2)) was compared with diethylenetriaminep
26 We use mass spectrometry to identify 374 diglycine-modified lysines on 236 ubiquitinated proteins
27 e C-terminal amino acid residues following a diglycine moiety on a small sulfur carrier protein, and
28 ion of the BK S6 alpha-helix from the unique diglycine motif at the position of the Kv hinge glycine.
29 one dynamics, indicate a bending motion at a diglycine motif connecting dimerization and cleavage reg
33 nds exclusively to the unanchored C-terminal diglycine motif of ubiquitin instead of conjugated polyu
34 s a deep binding pocket where the C-terminal diglycine motif of ubiquitin is inserted, thus explainin
35 with a beta-grasp fold and carboxy-terminal diglycine motif similar to ubiquitin, that form protein
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