A single residue switch reveals principles of antibody domain integrity.

Despite their importance for antibody architecture and design, the principles governing antibody domain stability are still not understood in sufficient detail. Here, to address this question, we chose a domain from the invariant part of IgG, the C2 domain. We found that compared with other Ig domains, the isolated C2 domain is a surprisingly unstable monomer, exhibiting a melting temperature of ∼44 °C.

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

The eukaryotic Hsp90 chaperone machinery comprises many co-chaperones and regulates the conformation of hundreds of cytosolic client proteins. Therefore, it is not surprising that the Hsp90 machinery has become an attractive therapeutic target for diseases such as cancer. The compounds used so far to target this machinery affect the entire Hsp90 system.

Tetramers are the activation-competent species of the HOCl-specific transcription factor HypT.

Hypochlorous acid (HOCl) is an important component of the immune system and is produced by neutrophils to kill invading microorganisms. The transcription factor HypT is specifically activated by HOCl by methionine oxidation and protects Escherichia coli cells from the detrimental effects of HOCl. HypT forms dodecameric ring-like oligomers.