The cool thing about parallel evolution is that it shows how complex phenotype can evolve from very different initial genetic conditions, highlighting the great power of evolution.
Source. Appears to be a compilation of several videos, presumably each with their own separate LA-UR, though these are not noted. Credited: "Video courtesy of the Los Alamos National Laboratory Archives", TODO how to search that archive online?
Frame: size: XS. Marking near bottom bracket: F/N GY17Z1327 DK: WGI GY17Z1327 F ES:BI-2339.
Seatpost: TODOdiameter. Measured in store 30.4mm after original stolen, although 2020 says 30.9. 30.4mm seemed to fit OK, and measuring with ruler gives 30.5/30.6, I don't think a 30.9 can possibly fit.
Sometimes you get annoyed to death with your bike not breaking or changing gears perfectly as you would like, and the people at the bike shop never do the job well enough.
The problem with bike shops is that the employees are already swamped with work, and they don't get paid any extra for doing more work.
Asa result, paradoxically, they are often happier, and respect you more if you are trying to get them to help you to fix your own bike!
Also, for the same reason, they don't have the time to go for a quick test ride after a fix to ensure that the bug was actually fixed.
So they ignore things that would obviously be huge ridability benefits (although they might not be obvious to newbie customers), for which customers would gladly pay more money for.
But you start to learn how to do stuff yourself and it feel amazing when you finally get there (after infinite trial and error).
Ciro dreams of a bike shop that actually calls you for the appointment and then teaches you how to fix the thing.
So the best strategy is to have a backup bicycle, and when your main one breaks, you just try to to the fix yourself. That means:
Then, if you fail to do the fix, that is OK, just take it to the bike shop, with the piece you've bought, and ask them to do it for you. At least this way you did not wastea golden opportunity to learn!
The model is extremely simple, but has been proven to be able to solve all the problems that any reasonable computermodel can solve, thus its adoption as the "default model".
Also interestingly, we see that both of those reaction require some extra energy to catalyse, one needing adenosine triphosphate and the other nADP+.
TODO: any mention of how much faster it makes the reaction, numerically?
Since this is an enzyme, it would also be interesting to have a quick search for it in the KEGG entry starting from the organism: www.genome.jp/pathway/eco01100+M00022We type in the search bar "thrA", it gives a long list, but the last entry is our "thrA". Selecting it highlights two pathways in the large graph, so we understand that it catalyzes two different reactions, as suggested by the proteinname itself (fused blah blah). We can now hover over:
the edge: it shows all the enzymes that catalyze the given reaction. Both edges actually have multiple enzymes, e.g. the L-Homoserine path is also catalyzed by another enzyme called metL.
the node: they are the metabolites, e.g. one of the paths contains "L-homoserine" on one node and "L-aspartate 4-semialdehyde"
Note that common cofactor are omitted, since we've learnt from the UniProt entry that this reaction uses ATP.
Aspartate kinase I / homoserine dehydrogenase I comprises a dimer of ThrA dimers. Although the dimeric form is catalytically active, the binding equilibrium dramatically favors the tetrameric form. The aspartate kinase and homoserine dehydrogenase activities of each ThrA monomer are catalyzed by independent domains connected by a linker region.
