Scholar Profile

Jose Rodriguez

Assistant Professor
Department of Chemistry and Biochemistry
University of California, Los Angeles
611 Charles E Young Drive East
539 Boyer Hall
Los Angeles, CA 90095-0001
Voice: 310-729-8416
Email: jrodriguez@mbi.ucla.edu
Personal Homepage
2017 Searle Scholar

Research Interests

Atomic Scale Interrogation of Protein Nano-assemblies

My group investigates the atomic level details that govern the behavior of protein macromolecules. To interrogate proteins at the atomic level, we develop new tools.

Our approaches make use of instruments including electron microscopes that can produce beams of electrons capable of extracting atomic information from small protein assemblies. Electrons interact so strongly with matter that protein assemblies just a few dozen molecules thick can produce signals from which near atomic resolution details can be interpreted.

Having the ability to peer into such small assemblies allows us to investigate challenging problems in structural biology. These problems include the nature of why and how proteins can self-assemble to form functional or sometimes disease causing structures. We can learn about how molecules are kept stored, inactivated, or mishandled by cells, with atomic level detail.

Two examples of these types of naturally occurring assemblies are cell-grown crystals and amyloid aggregates. In the case of amyloid, the aggregates that are formed go on to cause a number of diseases, which seem to be particularly harmful to the nervous system. These diseases include Alzheimer’s and Parkinson’s diseases, as well as a number of others.

Prion is a special type of amyoid disease that has particularly captured our interest. Prion is an infectious disease that relies on a protein to propagate, rather than on genetic material, like all other infectious diseases. Prion forms amyloid-like aggregates that can spread from person to person, cross between species, and be inherited. The true nature of how prion propagates requires a thorough structural understanding of the prion aggregate. Armed with new tools, we are now approaching the structure of Prion and other cellular protein assemblies that play key roles in biology and disease.