The formation of well-defined protein bioconjugates is critical for many studies and
technologies in chemical biology. Tried-and-true methods for accomplishing this typically …

Nα-terminal acetylation occurs in the yeast Saccharomyces cerevisiae by any of three N-
terminal acetyltransferases (NAT), NatA, NatB, and NatC, which contain Ard1p, Nat3p and …

Nα-terminal acetylation is one of the most common protein modifications in eukaryotes. The
COmbined FRActional DIagonal Chromatography (COFRADIC) proteomics technology that …

A highly reproducible, commercial and nonlinear, wide‐range immobilized pH gradient
(IPG) was used to generate two‐dimensional (2‐D) gel maps of [35S] methionine‐labeled …

We have used a modified CaMV 35S promoter to direct the expression of chimaeric genes
encoding human serum albumin (HSA) in transgenic potato and tobacco plants. To secrete …

Proline is unique among the 20 amino acids due to its cyclic structure. This specific
conformation imposes many restrictions on the structural aspects of peptides and proteins …

Protein N-myristoylation refers to the covalent attachment of myristate (C14: 0), via an amide
bond, to the amino-terminal Gly residue of a nascent polypeptide. This cotranslational …

Protein N-terminal acetylation is a major modification of eukaryotic proteins. Its functional
implications include regulation of protein–protein interactions and targeting to membranes …

High levels of nonfused chloramphenicol acetyltransferase, β-galactosidase, and β-
glucuronidase expressed under the control of new vector constructs of the polyhedrin …

The two cotranslational processes, cleavage of N-terminal methionine residues and N-
terminal1 acetylation, are by far the most common modifications, occurring on the vast …