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| Name |
Brunger, Axel T. |
| Location
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Stanford University |
| Primary Field
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Biophysics and Computational Biology |
| Secondary Field
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Biochemistry |
 Election Citation
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Brunger's concepts and strategies helped provide the foundation for much of modern structural biology. His determination of macromolecular structure of complex protein machinery by crystallography and NMR may ultimately lead to improved therapeutics. |
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Research Interests
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Early in his career, Brunger developed tools for interpreting X-ray crystallography diffraction data that revolutionized structural calculation. In his current research, Brunger applies his expertise in structural biology and biophysics to study the molecular mechanisms of synaptic proteins that enable nerve cell communication. Brunger and his collaborators employ biochemical reconstitution, biophysical analyses, and structural biology methods to investigate the molecular mechanisms of neuronal SNAREs, complexin, and synaptotagmin, as well as other factors involved in priming and pre-synaptic plasticity. His group used single-particle electron cryo-microscopy to determine structures of the supercomplex of SNAREs, the ATPase NSF, and the adapter protein a-SNAP. This subnanometer-resolution structure and functional studies have revealed the first glimpses of the molecular mechanism of NSF-mediated SNARE complex disassembly, which allows SNARE proteins to be recycled for the next round of synaptic vesicle fusion. Recently, Brunger studied the molecular architecture of proteins and protein complexes at the synapse and in synaptic vesicles using cryo-electron tomography, which led to the discovery of new protein-protein interactions. |
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