User talk:Axelbrunger

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

• avoid editing or creating articles about yourself, your family, friends, colleagues, company, organization, clients, or competitors;
• propose changes on the talk pages of affected articles (you can use the {{request edit}} template);
• disclose your conflict of interest when discussing affected articles (see Wikipedia:Conflict of interest#How to disclose a COI);
• avoid linking to your organization's website in other articles (see Wikipedia:Spam#External link spamming);
• do your best to comply with Wikipedia's content policies.

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)[reply]

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)[reply]

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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Appeals: If, after reading the guide to appealing blocks you believe you were blocked in error, then you may appeal this block by adding {{unblock|Your reason here}} below this notice. Jauerback^dude?/_dude. 15:32, 22 August 2022 (UTC)[reply]

Axel T. Brunger (born November 25, 1956) is a

Brunger is known for developing a computer program called X-PLOR,^[3]. 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.^[4]

Brunger introduced the RFree technique to cross-validate the model given the observed data.^[5]

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 ^[6] 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 ^[7]. 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.