Of the 20 ribosomally coded amino acid residues, lysine is the most frequently post-translationally modified, which has important functional and regulatory consequences. Here we report the ...

Industry standard tags contain lysine residues on both tag fragments, but lysine residues could themselves be implicated in the degradation pathway. “When we have a highly exposed lysine on the ...

Among them, the methylation of residues of lysine, which is one of the amino acids that make up histones, regulates the folding of genomic DNA and acts as a switch to turn gene transcription on ...

Instead of an S–S bridge connecting two cysteine residues, it consists of an N–O–S bridge between a lysine and a cysteine. (The “N” comes from a lysine residue’s NH 2 group ...

These are either co- or post-translational attachment to either the ε-amino group of lysine residues or the α-amino group of the N-terminus of target proteins. A variety of enzymes catalyze ...

Reaction of 1,3-BPG with lysine residues on proteins was expected to produce 3-phosphoglyceryl-lysine (pgK) modifications (Figure 1). After performing the GAPDH reaction using purified enzyme ...

One such category of epigenetic writers is histone methyltransferases, comprising enzymes that catalyze the transfer of a methyl group onto a lysine or arginine residue on histone tails.

The cleavage site at the junction of the A chain and the C-peptide contains a lysine residue, which is critical for cleavage. How does an abrogation of Cdkal1 in the beta cell result in a feeble ...

Lysine promises to make many more human proteins available to target with covalent drugs. This amino acid residue is nearly three times as abundant as cysteine in the body: an average of 32 ...

These negatively charged regions mediate strong binding of the antibodies to the positively charged arginine and lysine residues on PF4. 5 Panel A shows proteomic profiling of serum antibodies ...