Antibodies and Fc-fusion antibody-like proteins have become successful biologics
developed for cancer treatment, passive immunity against infection, addiction, and …

During the past year, many new antibody structures have been determined, increasing our
understanding of these immunologically important molecules. Of special interest are new …

The structure of an intact, anti-canine lymphoma monoclonal antibody (Mab231) 1 was
determined by molecular replacement and refined in a triclinic cell to an R-value of 20.9 …

The Fc portion of immunoglobulin G (IgG) expresses the biantennary complex type
oligosaccharides at Asn297 of the CH2 domain of each heavy chain with …

Ero1-α and endoplasmic reticulum (ER) oxidoreductases of the protein disulfide isomerase
(PDI) family promote the efficient introduction of disulfide bonds into nascent polypeptides in …

The flexibility of antibody molecules principally derives from the structure of the hinge region.
It has generally been accepted that the flexibility of the IgG hinge is necessary for …

Proteins are not static but are flexible molecules that can adopt many different
conformations. The HIV-1 protease is an important target for the development of therapies to …

The effects of sucrose and arginine on the conformational and storage stability of an IgG1
monoclonal antibody (mAb) were monitored by differential scanning calorimetry (DSC) and …

The methodology of regioselective cysteine pairings in synthetic multiple‐cystine peptides
has progressed in the past years to an efficiency that allows for at least three specific inter …

In the last 15 years substantial advances have been made to place isotope labels in native
and glycosylated proteins for NMR studies and structure determination. Key developments …