Allosteric proteins are the basic building blocks in the transmission of biological signals, allowing communication between and within cells, and from the extracellular environment to the cytosol. The modular organization of allosteric proteins, involving multiple domains and subunits, provides the structural scaffold for intricate regulation mechanisms mediated by networks of intra- and inter-subunit interactions.

In the Maillard lab, we are interested in understanding how individual domains in an allosteric protein complex cooperate to transduce a signal from one place to another. To answer this fundamental question, we use single molecule techniques in combination with mutagenesis, bulk biochemical and biophysical assays, and molecular dynamic simulations.

In particular, we are experts in optical tweezers, a single molecule mechanical manipulation technique we use to probe and monitor in real time the response of proteins upon force application.

Our ultimate research goal is to link physical and chemical properties of proteins based on conformation, dynamic motions, and stability to important functional processes such as catalysis, binding cooperativity and allostery.

Current Research Areas

1. Mechanism of Signal Transduction, focused on Protein Kinase A.

2. Regulation of Transcription by cAMP Receptor Protein.

3. Light-induced Conformational Changes in Circadian Clock Proteins.