Structural Biology – Multimedia

Understanding the molecular details of drug-target protein interactions is a critical component of the drug discovery process in the modern pharmaceutical industry.

The rapid growth of the therapeutic antibody market has increased the interest in modeling of the antibody structure and in understanding the factors that affect the function and the stability of antibodies.

Katja Arndt, University of Potsdam, speaking at Discovery Chemistry Congress 2015.

Jutta Eichler, University of Erlangen-Nuremberg, speaking at Discovery Chemistry Congress 2015.

The second virial coefficient of Human Serum Albumin (HSA) was measured using a SEC-MALS 20 detector connected to a Refractive Index concentration detector and an online differential viscometer. Two different buffer conditions, Phosphate buffer pH 7.4 and Citrate buffer pH 4.1 were used, which revealed interesting and contrasting data

Antibodies are central mediators of the immune system, IgG being the most dominant. Binding of IgG/antigen complexes to membrane-bound Fc? receptors triggers a cellular immune response. Alterations in the Fc portion of the antibody by introducing mutations can lead to complete abolition of Fc? receptor binding. This describes the development of a cellbased TR-FRET assay to determine the simultaneous binding of an antibody to its antigen and huFc?RIIIa present on different cells.

High purity protein is a common requirement for biochemical and structural studies. A common approach is to recombinantly express an affinity-tagged version of the protein of interest. This is, however, not always a viable option. This application note discusses protein purification workflow development for untagged proteins and introduce a new indicator of method performance, the purity quotient difference.

This poster demonstrates the ability of TTP Labtech’s mosquito® Crystal and mosquito® LCP to address the issues inherent in the automated set-up of protein crystallisation screen trials, without needing constant instrument configuration changes.

This poster demonstrates the ability of TTP Labtech’s mosquito® Crystal and mosquito® LCP to address the issues inherent in the automated set-up of protein crystallisation screen trials, without needing constant instrument configuration changes.