Taking careful lab notes

The red helices undergo local folding, transferring information between the two active sites of an aminoglycoside acetyltransferase. (Nat Struct Mol Biol 2011)

At the International Conference for Magnetic Resonance in Biological Systems dinner, Dallas, 2014

Studying an NMR spectrum

Centrifuging a sample

A phase diagram for protein allostery depends on the energies of conformational changes and inter-subunit interactions (Nat Chem Bio 2014)

The Mittermaier group arrives in Dallas, 2014

Breakfast Tacos: the best thing in Texas besides the ICMRBS conference

By combining NMR and calorimetry, we showed that a protein can fold in a cooperative all-or-none fashion, even if it is only marginally stable. (J Am Chem Soc 2010)

Dr. Meneses is congratulated by Dr. Mittermaier after having successfully defended his PhD

Analyzing data

Discussing results

NMR dynamics experiments can characterize protein ligand binding kinetics on faster timescales than those accessible by standard methods. (J Am Chem Soc 2009, J Biol Chem 2014)

Purifying samples by liquid chromatography

Setting up an ITC experiment

Folding of a C-terminal helix mediates allosteric communication between DNA- and peptide-binding sites in the PBX homeodomain. (J Mol Biol 2011)

Mittermaier group picture in front of the QANUC 500 MHz spectrometer


The Mittermaier lab studies biological macromolecules at the atomic level using NMR, calorimetry, and physical chemical theory. We seek to better understand how living systems operate and to apply this knowledge to problems in drug design and biocatalysis.

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