In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum
(ER), including the role of three types of covalent modifications: signal peptide removal, N …

Transport of newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi
complex is highly selective. As a general rule, such transport is limited to soluble and …

RNases are among the most stable proteins in nature. They even refold spontaneously after
heat inactivation, regaining full activity. Due to their stability and universal presence, they …

Ribonucleases (RNases) are a large number of enzymes gathered into different bacterial or
eukaryotic superfamilies. Bovine pancreatic RNase A, bovine seminal BS-RNase, human …

Disulfide Bonds in Protein Folding and Stability | Oxidative Folding of Proteins: Basic
Principles, Cellular Regulation and Engineering | Books Gateway | Royal Society of Chemistry …

Bovine seminal (BS) RNase, the unique natively dimeric member of the RNase super-family,
represents a special case not only for its additional biological actions but also for the …

Protein aggregation via 3D domain swap** is a complex mechanism which can lead to
the acquisition of new biological, benign or also malignant functions, such as amyloid …

Enzymes or proteins are commonly present in oligomeric forms for active biological
functions. The formation of protein oligomers, either in nature or by artificial means, can take …

Understanding protein folding under conditions similar to those found in vivo remains
challenging. Folding occurs mainly vectorially as a polypeptide emerges from the ribosome …

Protein self-association is a biologically remarkable event that involves and affects the
structural and functional properties of proteins. Indeed, some proteins, like hemoglobin …