Beta test of Neos mouse driver for C64OS.
Due to Commodores unfathomable dualing of the LMB and the data strobe compared to its msx sibling, there are compromises and issues to be worked around, but we've* got basic functionally. 📹👇
*Greg is doing the work, I'm just pestering him
Beta test of Neos mouse driver for C64OS.
Due to Commodores unfathomable dualing of the LMB and the data strobe compared to its msx sibling, there are compromises and issues to be worked around, but we've* got basic functionally. 📹👇
*Greg is doing the work, I'm just pestering him
pubs.acs.org/doi/10.1021/...
pubs.acs.org/doi/10.1021/...
www.biorxiv.org/content/10.1...
www.biorxiv.org/content/10.1...
#Commodore64 #C64 #C64Repair #RetroComputing #VintageComputers #C64Troubleshooting #CIA2 #HardwareRepair #RetroRepair
theoasisbbs.com/c64-repair-t...
#Commodore64 #C64 #C64Repair #RetroComputing #VintageComputers #C64Troubleshooting #CIA2 #HardwareRepair #RetroRepair
theoasisbbs.com/c64-repair-t...
www.biorxiv.org/content/10.1...
Check out what we (and by we I mean my labmates) worked so hard on and got to learn about how proteins interact in the pathway that develops and sends iron-sulfur clusters to so many important proteins!
www.biorxiv.org/content/10.1...
Check out what we (and by we I mean my labmates) worked so hard on and got to learn about how proteins interact in the pathway that develops and sends iron-sulfur clusters to so many important proteins!
www.youtube.com/watch?v=cia2...
www.youtube.com/watch?v=cia2...
Nar1 engages the CIA targeting complex through a bipartite binding mechanism:
• a conserved electrostatic interface anchors Nar1 to a conserved acidic face of Cia1
• Nar1's divergent targeting complex recognition motif exploits the client recruitment site at the Cia1-Cia2 interface
Nar1 engages the CIA targeting complex through a bipartite binding mechanism:
• a conserved electrostatic interface anchors Nar1 to a conserved acidic face of Cia1
• Nar1's divergent targeting complex recognition motif exploits the client recruitment site at the Cia1-Cia2 interface