Metalloenzymes are central to a wide range of essential biological activities, including
nucleic acid modification, protein degradation, and many others. The role of metalloenzymes …

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 …

Methionine aminopeptidase (MAP) is a ubiquitous, essential enzyme involved in protein N-
terminal methionine excision. According to the generally accepted cleavage rules for MAP …

Elicitation of antibodies against targets that are immunorecessive, cryptic, or transient in their
native context has been a challenge for vaccine design. Here we demonstrate the elicitation …

Metalloaminopeptidases remove the N-terminal amino acid from proteins or small
oligopeptides. This modification or truncation process can occur either co-translationally or …

This Handbook on Metalloproteins focuses on the available structural information of proteins
and their metal ion coordination spheres. It centers on the metal ions indispensable for life …

The book is a technical guide for chemists and spectroscopists, and presents a concise
description of magnetic circular dichroism (MCD) spectroscopy and how it has advanced the …

Researchers in the post‐genome era are confronted with the daunting task of assigning
structure and function to tens of thousands of encoded proteins. To realize this goal, new …

Protein synthesis is initiated by methionine in eukaryotes and by formylmethionine in
prokaryotes. N‐terminal methionine can be co‐translationally cleaved by the enzyme …

The removal of the N-terminal methionine from proteins and peptides is dependent upon a
novel class of proteases typified by the dinuclear metalloenzyme methionine …