This situation is the most bizarre thing ever. The dude was fired in 2020, but he refused to be fired, and because he has the company seal, they can't fire him. He is still going to the office as of 2022. It makes one wonder what are the true political causes for this situation. A big warning sign to all companies tring to setup joint ventures in China!
Discovered by Marie Curie when she noticed that there was some yet unknown more radioactive element in their raw samples, after uranium and polonium, which she published 6 months prior, had already been separated. Published on December 1989 as: Section "Sur une nouvelle substance fortement radio-active, contenue dans la pechblende".
The uranium 238 decay chain is the main source of naturally occurring radium.
Contains the University of Cambridge, that's about it really, from that everything follows.
The city appear to exist there because it was a convenient crossing of the Cam. It also lies near the start of the ancient navigable section TODO towards north or south? Castle hill also offered a convenient fortification location near the river, and is part of the reason for the early Roman settlement. The original bridge was presumably in the current Magnalene bridge, just under the castle hill.
TODO why did the University of Oxford scholars flee to after the The hanging of the clerks in 1209? Why not anywhere else?
To Ernest Lawrence for the cyclotron.
Suppose we have a given permutation group that acts on a set of n elements.
If we pick k elements of the set, the stabilizer subgroup of those k elements is a subgroup of the given permutation group that keeps those elements unchanged.
Note that an analogous definition can be given for non-finite groups. Also note that the case for all finite groups is covered by the permutation definition since all groups are isomorphic to a subgroup of the symmetric group
TODO existence and uniqueness. Existence is obvious for the identity permutation, but proper subgroup likely does not exist in general.
Group of all permutations.
In Qiskit at: qiskit/hello.py.
- 2008-08-18: bitcoin.org registered
- 2008-10-31: first public announcement at www.metzdowd.com/pipermail/cryptography/2008-October/014810.html by satoshi@vistomail.com
- 2009-01-03: Genesis block mined
- 2009-01-11: First block not mined by Satoshi
- 2009-01-12: First Bitcoin transactoin
- 2010-05-18: the first of Laszlo's pizzas at about $0.0045 / BTC
- 2010-07-17: first trade happes on Mt. Gox at $0.04951 / BTC: cryptopotato.com/10-years-ago-first-bitcoin-trade-on-mt-gox-for-0-05-per-btc/
- 2014: OP_RETURN goes live
Group of even permutations.
Note that odd permutations don't form a subgroup of the symmetric group like the even permutations do, because the composition of two odd permutations is an even permutation.
NCBI entry: www.ncbi.nlm.nih.gov/gene/945803.
Part of a reaction that produces threonine.
This protein is an enzyme. The UniProt entry clearly shows the chemical reactions that it catalyses. In this case, there are actually two! It can either transforming the metabolite:Also interestingly, we see that both of those reaction require some extra energy to catalyse, one needing adenosine triphosphate and the other nADP+.
- "L-homoserine" into "L-aspartate 4-semialdehyde"
- "L-aspartate" into "4-phospho-L-aspartate"
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+M00022 We 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 protein name itself (fused blah blah). We can now hover over:Note that common cofactor are omitted, since we've learnt from the UniProt entry that this reaction uses ATP.
- 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"
If we can now click on the L-Homoserine edge, it takes us to: www.genome.jp/entry/eco:b0002+eco:b3940. Under "Pathway" we see an interesting looking pathway "Glycine, serine and threonine metabolism": www.genome.jp/pathway/eco00260+b0002 which contains a small manually selected and extremely clearly named subset of the larger graph!
But looking at the bottom of this subgraph (the UI is not great, can't Ctrl+F and enzyme names not shown, but the selected enzyme is slightly highlighted in red because it is in the URL www.genome.jp/pathway/eco00260+b0002 vs www.genome.jp/pathway/eco00260) we clearly see that thrA, thrB and thrC for a sequence that directly transforms "L-aspartate 4-semialdehyde" into "Homoserine" to "O-Phospho-L-homoserine" and finally tothreonine. This makes it crystal clear that they are not just located adjacently in the genome by chance: they are actually functionally related, and likely controlled by the same transcription factor: when you want one of them, you basically always want the three, because you must be are lacking threonine. TODO find transcription factor!
The UniProt entry also shows an interactive browser of the tertiary structure of the protein. We note that there are currently two sources available: X-ray crystallography and AlphaFold. To be honest, the AlphaFold one looks quite off!!!
By inspecting the FASTA for the entire genome, or by using the NCBI open reading frame tool, we see that this gene lies entirely in its own open reading frame, so it is quite boring
From the FASTA we see that the very first three Codons at position 337 arewhere
ATG CGA GTG
ATG
is the start codon, and CGA GTG should be the first two that actually go into the protein:ecocyc.org/gene?orgid=ECOLI&id=ASPKINIHOMOSERDEHYDROGI-MONOMER mentions that the enzime is most active as protein complex with four copies of the same protein:TODO image?
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.
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