User talk:Axelbrunger

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Happy editing! Amkilpatrick (talk) 07:44, 22 August 2022 (UTC)

COI

Hello, Axelbrunger. We welcome your contributions, but if you have an external relationship with the people, places or things you have written about on the page Axel T. Brunger, you may have a conflict of interest (COI). Editors with a conflict of interest may be unduly influenced by their connection to the topic. See the conflict of interest guideline and FAQ for organizations for more information. We ask that you:

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In addition, you are required by the Wikimedia Foundation's terms of use to disclose your employer, client, and affiliation with respect to any contribution which forms all or part of work for which you receive, or expect to receive, compensation. See Wikipedia:Paid-contribution disclosure.

Also, editing for the purpose of advertising, publicising, or promoting anyone or anything is not permitted. Thank you. Amkilpatrick (talk) 07:49, 22 August 2022 (UTC)

Thank you for your note. In my edits I wanted to correct my page (Axel T. Brunger) and provide some updates. I did not realize that this constitutes a conflict of interest. I just tried to undo the changes, but this created a mess. Thus, I would like to kindly request that you consider my changes as proposed changes and accept them. Thank you.

Best,

Axel T. Brunger Axelbrunger (talk) 15:22, 22 August 2022 (UTC)

August 2022

This account has been blocked indefinitely from editing Wikipedia because the username, Axelbrunger, matches the name of a well-known, living person.

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Edit request

Axel T. Brunger (born November 25, 1956) is a German American biophysicist. He is Professor of Molecular and Cellular Physiology at Stanford University, and a Howard Hughes Medical Institute Investigator. He served as the Chair of the Department of Molecular and Cellular Physiology (2013–2017).

Early life

Brunger was born in Leipzig, Germany, on November 25, 1956. He graduated with a degree in Physics and Mathematics from the University of Hamburg in 1977. He completed his Diplom in Physics from the University of Hamburg in 1980. He completed his PhD in Biophysics from Technical University of Munich in 1982, advised by Klaus Schulten.

Academic career

Brunger held a NATO postdoctoral fellowship to work with Martin Karplus at Harvard University, where he subsequently became a research associate in the Department of Chemistry after a brief return to Germany. He joined the Molecular Biophysics and Biochemistry department at Yale University in 1987 and moved to Stanford University in 2000. He also holds an appointment as Investigator in the Howard Hughes Medical Institute. In 1995, he was awarded the Röntgen Prize for Biosciences from the University of Würzburg. In 2003, he received the Gregori Aminoff Award of the Royal Swedish Academy. In 2005, he was elected member of the National Academy of Sciences United States National Academy of Sciences. In 2011, he received the DeLano Award of the American Society for Biochemistry and Molecular Biology, and in 2014, he received both the Bernard Katz Award of the Biophysical Society and the Carl Hermann Medal of the German Crystallographic Society. In 2016, he received the Trueblood Award of the American Crystallographic Association. In 2021, he was elected member of the American Academy of Arts and Sciences.

Research

Brunger is known for developing a computer program called X-PLOR,. X-PLOR makes use of a method called simulated annealing in conjunction with molecular dynamics to refine protein structures. X-PLOR was the first time a modern optimization technique was applied to the problem of crystallographic refinement. X-PLOR was initially motivated by efforts in interpreting NMR data (collaboration with Marius Clore) which has been extended by Clore's continued development of XPLOR-NIH. In the mid-1990s, Brunger's team extended X-PLOR into a complete system to determine structures CNS, capable of performing a series of steps necessary for crystallography structure determination, such as obtaining phases from experimental data and molecular replacement phasing from known homologous structures.

Brunger introduced the RFree technique to cross-validate the model given the observed data.

Since the mid-1990s, Brunger has applied his expertise in structural biology to study the molecular mechanisms of synaptic proteins that enable nerve cell communication by neurotransmission. At the time, scientists knew that the SNARE protein complex involved in neurotransmission consisted of synaptobrevin, syntaxin-1, and SNAP-25. Synaptic vesicles carry synaptobrevin, along with neurotransmitters, to the nerve cell membrane’s inner face, which contains syntaxin and SNAP-25. As the respective SNAREs zip up, they fuse the synaptic vesicle membrane and the nerve cell membrane, releasing neurotransmitter from the pre-synaptic neuron. In 1998, Brunger and coworkers showed that the corkscrew-shaped SNARE proteins assemble into quartets of one syntaxin-1, one synaptobrevin, and two SNAP-25 helices (collaboration with Reinhard Jahn). The proteins all lie in parallel, with their heads pointing in the same direction, to promote membrane fusion.

Since moving to Stanford University in 2000, Brunger developed a reconstituted system that enables them to study synaptic fusion at greater level of detail than possible in live neurons. The team studied the molecular mechanism of neuronal SNAREs, complexin, and synaptotagmin, as well as other factors involved in priming and pre-synaptic plasticity. In 2015 and 2018, Brunger’s team used single particle electron cryo-microscopy to determine structures of the supercomplex of SNAREs, the ATPase NSF, and the adapter protein α-SNAP . These structures, along with functional studies, revealed first glimpses of the molecular mechanism of NSF-mediated SNARE complex disassembly, which allows SNARE to be recycled for the next round of synaptic vesicle fusion. In 2015 and 2017, Brunger’s team determined atomic-resolution structures of complexes of the calcium sensor synaptotagmin-1, the neuronal SNARE complex, and the regulator complexin. These structures suggested an unlocking mechanism that is triggered by calcium binding to the synaptotagmin molecules, leading to SNARE complex zippering and membrane fusion.

References

Axelbrunger (talk) 22:10, 23 August 2022 (UTC)

I think this request belongs at Talk:Axel T. Brunger? ---Another Believer _(Talk) 17:59, 31 August 2022 (UTC)

Correct. Can you please move it there? Axelbrunger (talk) 18:07, 31 August 2022 (UTC)

I have also moved the edit request template. Rusalkii (talk) 04:40, 24 September 2022 (UTC)