Allen Wu Updated +Created
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!
Video 1.
ARM Fired ARM China’s CEO But He Won’t Go by Asianometry (2021)
Source.
Radium Updated +Created
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.
Video 1.
The epic story of radium by Institut de Radioprotection et de Sûreté Nucléaire (2013)
Source.
Cambridge Updated +Created
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?
1932 Nobel Prize in Physics Updated +Created
Stabilizer (group) Updated +Created
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.
Symmetric group Updated +Created
100,000 Genomes Project Updated +Created
3D rigid body dynamics simulator Updated +Created
Bell circuit Updated +Created
A quantum circuit which when fed with input produces the Bell state.
Figure 1.
Quantum circuit that generates the Bell state
. Source.
The fundamental intuition for this circuit is as follows.
First the Hadamard gate makes the first qubit be in a 50/50 state.
Then, the CNOT gate gets controlled by that 50/50 value, and the controlled qubit also gets 50/50 chance as a result.
However, both qubits are now entangled: the result of the second qubit depends on the result of the first one. Because:
  • if the first qubit is 0, cnot is not active, and so the second qubit remains 0 as its input
  • if the first qubit is 1, cnot is active, and so the second qubit is flipped to 1
Loopholes in Bell test experiments Updated +Created
FreeBSD Updated +Created
History of Bitcoin Updated +Created
2D Ising model Updated +Created
Alternating group Updated +Created
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.
Mark Zuckerberg Updated +Created
E. Coli K-12 MG1655 gene thrA Updated +Created
The second gene in the E. Coli K-12 MG1655 genome. Part of the E. Coli K-12 MG1655 operon thrLABC.
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:
  • "L-homoserine" into "L-aspartate 4-semialdehyde"
  • "L-aspartate" into "4-phospho-L-aspartate"
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+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:
  • 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.
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 are
ATG CGA GTG
where 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:
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.
TODO image?
Interface Message Processor Updated +Created
Principles of AGI Updated +Created

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