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David Casas-Mao is a structural biologist with over 14 years of expertise in protein purification and biophysical characterization. He holds a B. S. degree in Chemical Biology from the University of California, Berkeley. In Prof. David Wemmer’s lab at UCB, he used 900 MHz multidimensional nuclear magnetic resonance methods to determine the structure and dynamics of two domains of the bacterial transcription initiation factor sigma54 bound to upstream DNA elements or to the ATPase domain of the transcriptional activator NtrC1.
David completed his doctoral degree working under Dr. David Scott (University of Nottingham) while based at the Research Complex in Harwell, the Diamond Light Source Oxfordshire site of the UK national synchrotron facility. Here, he significantly advanced the structural and biophysical characterization of three proteins involved in bacterial silver resistance, using cryo-EM, SAXS, ITC, SANS, CD spectroscopy, and analytical ultracentrifugation. He studied mainly SilP, an ATPase Ag+ efflux pump that confers silver resistance to Gram-negative bacteria, solving the crystal structure of its Heavy Metal Binding Domain bound to 3 silver atoms to 1.5 Å resolution. This allowed a precise description of its ligand-binding core and identified the HMBD molecular architecture as a novel, conserved protein fold.
In his postdoc under Prof. Michelle Peckham at the University of Leeds, he studied how mutations in non-muscle myosin drive human disease using cryo-EM, cryo-ET, confocal, and super-resolution microscopy, shedding new light into myosin dysregulation and its associated physiological syndromes. Using single particle cryo-EM, he solved the structure of whole Smooth Muscle Myosin in the inactive form that revealed the stabilizing interactions present in the inactive state, providing a framework to understand its function and mutational effects. This structure published in the journal Nature elucidated how the inhibited state is relieved upon phosphorylation, explaining for the first time why phosphorylation of both regulatory light chains is required to impart full myosin activation.
David has acquired an extensive background in a diverse set of structural biology, biophysics, and molecular biology methods that have equipped him with a powerful multidisciplinary toolkit to translate his scientific knowledge into biopharmaceutical applications.
At General Proximity, David is a Scientist II on the platform team, using cryo-EM to investigate the structure and biochemical properties of target proteins deemed “undruggable” by conventional approaches. In his free time, he enjoys film photography, discovering cinema classics, watching/playing soccer, and exploring new restaurants.
