Robert M. Stroud

Biosketch

Robert Stroud is Professor of Biochemistry and Biophysics, at the University of California in San Francisco (UCSF). He is a structural biologist recognized for discovery of new paradigms in membrane protein biology including mechanisms of aquaporins, Rh factors, membrane protein synthesis and protein insertion through translocons, unfolded protein response, transporters, and the structural basis for paradigms in enzyme mechanisms including trypsin, viral proteases, polyketide synthases and cancer target thymidylate synthase. Dr. Stroud was born and grew up in Stockport England and graduated from the University of Cambridge (UK) with a BA (1964) in Natural Sciences, MA (1968) and from University of London with a Ph.D in crystallography of nucleoside antibiotics (JD Bernal advisor). His postdoctoral was at Caltech (1968-1971) where he determined the first structure of the enzyme trypsin (with Richard Dickerson). He was appointed assistant and associate professor of chemistry at Caltech where he started to define the structural basis for the acetylcholine receptor, an integral membrane protein complex at a time before any structures of membrane proteins had been determined. He has been president of the US Biophysical society, and is a member of the US National Academy of Sciences, and the American Academy of Arts and Sciences.

Research Interests

Stroud's current research focuses on fundamental transmembrane biology. Packaging of neurotransmitters in presynaptic cells and neuronal signaling is a focus. He is defining receptor and transceptor function, mechanisms of membrane protein insertion and assembly, transmembrane transport, fundamentals of cellular signaling and communication across cell membranes at the molecular and structural levels. The fundamental mechanisms of, and then the regulation of voltage dependent activation of ion channels is a focus. Identifying and then 'pulling out' molecular machines and interactions that are the key to major diseases, particularly due to Mycobacterium tuberculosis, HIV, and COVID19 are a burgeoning new trend. Dr. Stroud determined the first structure of any water channel at atomic resolution and defined the basis for selectivity in the water/glycerol family. He similarly defined the first structural basis of ammonia channels of the Rh family. Continuing interests spring from his long term association with the Signal Recognition Particle basis for insertion, and then assembly of membrane proteins. Dr Stroud defined fundamental aspects of the unfolded response by determining structures that showed how such proteins, perhaps due to overexpression in response to disease or injury, are recognized and signal to rescue the extra demand, or chose cell death.