I am looking for a highly talented postdoc to join my lab to study ATP-dependent AAA machines using structural biology, biochemistry, and mass spectrometry. Please apply through the following link: https://t.co/LNqxDbobOx For more information, visit: https://t.co/Gb7o13Hmti
Now out: our collaboration with Qi Ouyang and Yuhai Tu. Direct cryo-EM observation of coupling between subunits in clock protein KaiC. Each protein complex acts a cooperative switch and the daily phosphorylation cycle changes the free energy of the states.
https://t.co/BKP76szbhY
We are happy to share our latest work about the E3 ligase UBR5: Two manuscripts @CellPressNews!
https://t.co/GpGIHkkMlH
https://t.co/6FIhKNEnWS
The result of fantastic collaborative efforts with the Ebert and @RapeLab. Thanks to the many contributing authors! #cryoEM#ubiquitin
In our new paper https://t.co/IMgZOX3WKY we unexpectedly find that dimerization domains of bHLH TFs interface with histones specifying E-box binding. A big shoutout to the collaborators! @partchlab @jsmenet@Beatfierz@johannes_zuber@SchubelerLab@RalphSGrand @PriyaCrosby
Finally online! https://t.co/NTioamRtIb. This was a collaboration between @partchlab and @LanderLab where we structurally characterized the differences between the circadian phase-opposite phosphoforms of the cyanobacterial clock protein KaiC using cryoEM. Congrats @Sandate_C!
Plastic pollution endangers wild and human life more every day. Can we clean this up? What to do with the waste once collected? With the Ellington,@at_lynd, and Zhang labs, we’ve developed an enzyme that can break down PET plastic: FAST PETase. https://t.co/rsICQ0ATUk @EnergyUT
Interested in the structural biology of circadian oscillators and AAA+ proteins? Our recent preprint describes structural changes throughout KaiC’s phosphorylation cycle that underlie binding to KaiB.
@partchlab @theREALJeffSwan@liwangandy@susanksgolden It was a real joy working on this project!! KaiC is such a fascinating protein, and we got to solve cool new structures of it. Thanks for the great collaboration.