Statement of Support for Asian Communities

Dr. Christina Hull, in her capacity as Chair of the Diversity, Equity, and Inclusion Committee for the Integrated Program in Biochemistry (IPiB) issued the following statement in response to the regrettable recent rise in hate …

Solving New Proteins Structure with NMR Spectroscopy

Proteins are linear chains of amino acids that fold into complex three-dimensional structures associated with particular functions. Extensive structural analyses of proteins by X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy have revealed that many proteins are modular, and consist of domains that fold independently. If an amino acid sequence folds into a particular structure, it is a safe bet that a similar sequence in a second protein will adopt a similar structure. Hundreds of unique modules have been defined and archived in databases that allow prediction of structure and function on the basis of amino acid sequence. However, sequences still exist for which structure cannot be predicted. Such was the case for myeloid-derived growth factor (MYDGF), a protein of ~145 amino acids present in nearly every tissue and cell in the human body and in organisms as distant from humans as slime molds.

A Trojan Horse? Immune cells ferry deadline fungus from mouse lung into the blood

A report today (June 27) in PLOS Pathogens shows how inhaled fungal spores exit the lung and trigger a fatal infection in mice. The study solves a mystery of mycology: Why are spores of a certain fungal strain deadly while the yeast form of that same fungus is harmless? Study leader Christina Hull, professor of biomolecular chemistry and medical microbiology and immunology at the University of Wisconsin–Madison, focuses on Cryptococcus, the most deadly inhaled fungus. The short answer, she says, is that lung macrophages abandon their posts as bodyguards and begin smuggling spores into the bloodstream.

Blockages in nerve-cell protein ‘factory’ ipmlicated in neurodegenerative disease

A molecular basis underlying the neurodegenerative condition hereditary spastic paraplegia (HSP) has been identified in a study by University of Wisconsin School of Medicine and Public Health researchers. The research, published in Cell Reports, shows how a mutation in the TFG gene – one of several linked to HSP – impairs neurons from forming the structures needed to transmit signals properly.