Disulfide bond formation is probably involved in the biogenesis of approximately one third of
human proteins. A central player in this essential process is protein disulfide isomerase or …

Summary Immunoglobulin G4 (IgG4) antibodies have been known for some time to be
functionally monovalent. Recently, the structural basis for this monovalency has been …

Abstract The Escherichia coli OxyR transcription factor senses H 2 O 2 and is activated
through the formation of an intramolecular disulfide bond. Here we present the crystal …

Protein thiol reactivity generally involves the nucleophilic attack of the thiolate on an
electrophile. A low p K a means higher availability of the thiolate at neutral pH but often a …

▪ Abstract Disulfide bonds formed between pairs of cysteines are important features of the
structure of many proteins. Elaborate electron transfer pathways have evolved Escherichia …

Background: Exposure of biomacromolecules to ionising radiation results in damage that is
initiated by free radicals and progresses through a variety of mechanisms. A widely used …

▪ Abstract Disulfide bonds in proteins play various important roles. They are either formed as
structural features to stabilize the protein or are found only transiently as part of a catalytic or …

Oxidation of cysteine pairs to disulfide requires cellular factors present in the bacterial
periplasmic space. DsbB is an E. coli membrane protein that oxidizes DsbA, a periplasmic …

The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the
study of oxidative protein folding. Oxidative protein folding refers to the composite process …

DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is
thought to function as a disulfide bond isomerase during oxidative protein folding in the …