Faculty Courtesy Appointments
Member, National Academy of Sciences
Research Interest: Axel Brunger's goal is to understand the molecular mechanism of synaptic neurotransmission. He is particularly interested in the structure, function, and dynamics of key players in the synaptic vesicle fusion machinery. His lab is also working on the mechanism of action of clostridial neurotoxins that target this machinery. Other projects include the ATPases of the AAA family that are involved in protein complex disassembly and degradation. A molecular understanding of these complex protein m.
Christopher Barnes is a structural biologist with expertise in cryo-electron microscopy (cryoEM), X-ray crystallography, and X-ray free electron laser (XFEL) methods. His lab is interested in how enveloped viruses (e.g., HIV-1, HIV-2, coronaviruses, and emerging zoonotic viruses) interact with host protein receptors for entry and how the immune system responds to these outside invaders. Of particular interest is translating knowledge of the structural correlates of antibody-mediated neutralization into the rational development of protective antibodies with improved potencies and/or are resistant to viral mutations, design of viral entry and replication inhibitors, and using structure-based immunogen design to improve protein-based vaccine candidates.
Research Interest: Molecular motors lie at the heart of biological processes from DNA replication to vesicle transport. My laboratory seeks to understand the physical mechanisms by which these nanoscale machines convert chemical energy into mechanical work.
Research Interest: My primary research interests are in computational biology, with an emphasis on spatial structure and dynamics at the molecular and cellular levels. My work, usually carried out in close collaboration with experimentalists, spans fields ranging from biochemistry and cell biology to parallel computing, image processing, and machine learning.
I joined the Stanford faculty in 2014, after more than a decade in industry. I enjoy working with students and postdocs from a wide variety of disciplines, including computer science, applied math, electrical engineering, biophysics, bioengineering, and chemistry. If you’d like to join me in building a new research group, please contact me. Please also contact me if you’re interested in collaborating, whether you’re in academia or at a company.
Research Interest: We are interested in the structure, dynamics and function of eukaryotic transport proteins mediating ions and major nutrients crossing the membrane, the kinetics and regulation of transport processes, the catalytic mechanism of membrane embedded enzymes and the development of small molecule modulators based on the structure and function of membrane proteins.
E. Peter Geiduschek
Biography: E. Peter Geiduschek received his Ph.D. from Harvard University. He was awarded a Guggenheim Fellowship and has served on the editorial boards of several scientific journals. Dr. Geiduschek is a member of the National Academy of Sciences and the American Academy of Arts and Sciences and is also a fellow of the American Association for the Advancement of Science and the American Academy of Microbiology
Research Interest: The central theme of my research has been the enzymology of gene regulation, specifically of transcriptional regulation and its principal focus has been on fundamental mechanisms, approached from a molecular genetic and biochemical perspective. It is now widely appreciated that the transcriptional apparatus of all cells (archaeal, bacterial and eukaryotic) has common evolutionary roots. It follows that transcription-regulatory mechanisms should also share certain broadly similar mechanistic features. In that spirit, my laboratory worked in parallel with bacteria and their viruses, with eukaryotes, and with archaea. As a member of Roger Kornberg’s group, the principal focus of my current thinking is on RNA polymerase II and chromatin.
Research Interest: We are currently investigating mechanisms involved in synaptic transmission and synaptogenesis using electron microscope tomography in ways that provide in situ 3D structural information at macromolecular resolution.
Research Interest: Many of the wonders associated with biomolecules rest in their functionality, but before they can carry out any function, many of these molecules must accomplish another amazing feat: them must first assemble themselves. Moreover, these molecules must build complex structures quickly and reliably. It is intriguing to consider how one can design molecules to self assemble. Actually, this is an extremely old problem: for billions of years, Nature has been honing its skills at molecular design. Can we benefit from Nature's billion year investment in the R & D of molecular self assembly?
Naima Sharaf got her undergraduate degree in Chemistry at the University of North Carolina-Chapel Hill. She carried out her Ph.D. studies at the University of Pittsburgh in the lab of Dr. Angela Gronenborn where she used fluorine solution NMR to understand inhibitor-induced conformational changes with HIV-1 reverse transcriptase. To expand her structural biology skill set, she undertook postdoctoral training at Caltech in the lab of Dr. Doug Rees where she characterized the structure and function of the Neisseria meningitides methionine ABC transport system using x-ray crystallography and single-particle cryo-EM. This research sparked Dr. Sharaf's current interest in lipoproteins, particularly their roles in bacterial physiology and potential in vaccine design. Research in the Sharaf Lab bridges biochemistry, biology, microbiology, and immunology to translate lipoprotein research into therapeutics.