Our new study of how tau fibrils with the Alzheimer’s disease structure bind lipid membranes just came out at JACS! Check it out here https://t.co/89kef3QWr9
Check out our new NMR study of how a dynamic polar network in the SARS-CoV-2 E protein mediates proton and calcium ion binding! https://t.co/nRsXt9kvpI
A tau construct (297-391) reported to replicate the Alzheimer’s paired helical filament structure instead forms non-twisting fibrils under high MgCl2 concentrations. Our atomic-resolution ssNMR structure reveals how this structure is stabilized. DOI: 10.1073/pnas.2310067120
Using solid-state NMR, we solved the open structure of the SARS-CoV-2 E viroporin. Compared to the closed state, the open state has a wider N-terminal pore and a tighter C-terminal region, suggesting the cation conduction mechanism of this channel. DOI: 10.1126/sciadv.adi9007
Many Hong lab members attended the Protein Society Meeting here in Boston this week. It was an excellent meeting, with great science and great interactions.
19F NMR data shed light on how three phenylalanine residues in the envelope protein of the SARS-CoV-2 virus controls the opening of this cation channel. https://t.co/FSHK0iMTgI
The Envelope Protein of SARS-CoV-2 is a viroporin that may induce severe inflammation for COVID. ssNMR+19F gave us the structure and an aromatic gating mechanism regulating this viroporin (💊🎯), induced by calcium and acidic pH. @MeiHongLab#GlobalnmrTC2022 +poster below
Solid-state NMR data reveal that the tau protein associates with microtubules through a pseudorepeat domain R', while a proline-rich region and an R1 domain remain mobile. https://t.co/bb8cKxEG5F
Jammy plants! See how impaired methylation of pectins lead to dwarf plants because of significant changes in the cell wall structures, as detected by solid-state NMR https://t.co/BCxWXhRfU0
The small methyl group can do big things! Solid-state NMR reveals how de-methylation of pectins in plant cell walls dramatically affect wall structure and slow plant growth. https://t.co/6pgH03eeSm
Solid-state NMR data reveal that two versions of the protein tau are fluently mixed in the neurotoxic tangles in the Alzheimer brain, defining the structure of the third dimension of these fibrils. https://t.co/zg1uxruc4O
19F NMR illuminates how acidic pH and calcium ions change the sidechain conformation of two aromatic residues in the SARS-CoV-2 envelope protein to permit cation conduction. https://t.co/aLS6tarEfU
Second structure of EmrE determined by NMR, finally showing this transporter in action, using pH-controlled alternating access to pump out toxic compounds! https://t.co/SWBANCkAPC
https://t.co/q38OSebGaE