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.
To Ernest Lawrence for the cyclotron.
But recent developments are making it too exciting to ignore.
Really weird and obscure company, good coverage: thequantuminsider.com/2020/02/06/quantum-computing-incorporated-the-first-publicly-traded-quantum-computing-stock/
Publicly traded in 2007, but only pivoted to quantum computing much later.
Quantum numbers appear directly in the Schrödinger equation solution for the hydrogen atom.
However, it very cool that they are actually discovered before the Schrödinger equation, and are present in the Bohr model (principal quantum number) and the Bohr-Sommerfeld model (azimuthal quantum number and magnetic quantum number) of the atom. This must be because they observed direct effects of those numbers in some experiments. TODO which experiments.
E.g. The Quantum Story by Jim Baggott (2011) page 34 mentions:This refers to forbidden mechanism. TODO concrete example, ideally the first one to be noticed. How can you notice this if the energy depends only on the principal quantum number?
As the various lines in the spectrum were identified with different quantum jumps between different orbits, it was soon discovered that not all the possible jumps were appearing. Some lines were missing. For some reason certain jumps were forbidden. An elaborate scheme of ‘selection rules’ was established by Bohr and Sommerfeld to account for those jumps that were allowed and those that were forbidden.
Quantum Numbers, Atomic Orbitals, and Electron configurations by Professor Dave Explains (2015)
Source. He does not say the key words "Eigenvalues of the Schrödinger equation" (Which solve it), but the summary of results is good enough. Quantum Processes and Computation course of the University of Oxford Updated 2025-07-01 +Created 1970-01-01
2022 page: www.cs.ox.ac.uk/teaching/courses/2022-2023/quantum/ (archive). Assignments are available:
- www.cs.ox.ac.uk/people/aleks.kissinger/courses/qpc2022/assignment1.pdf
- www.cs.ox.ac.uk/people/aleks.kissinger/courses/qpc2022/assignment2.pdf
- www.cs.ox.ac.uk/people/aleks.kissinger/courses/qpc2022/assignment3.pdf
- www.cs.ox.ac.uk/people/aleks.kissinger/courses/qpc2022/assignment4.pdf
- www.cs.ox.ac.uk/people/aleks.kissinger/courses/qpc2022/assignment5.pdf
- www.cs.ox.ac.uk/people/aleks.kissinger/courses/qpc2022/assignment6.pdf
2022 lecturer: Aleks Kissinger
The course would be better named ZX-calculus as it appears to be the only subject covered.
Group of all 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.
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+.
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 GTGATG 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.
- 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
Future self, answer these.
20 years
- 2018-2038: are companies offering free full genome decoding just to get your genomic data and sell it to pharma companies?Someone like Ciro then creates an open source genomic database funded by health organizations that publishes genomes + phenotypes anonymously. Genome to phenotype analytics go crazy big.
40 years:
- 2017-2057: was human level AI reached (by non-bio devices :-)), even if very slow?
- 2017-2057: did China become democratic?
- 2018-2058: did impressive brain-computer interfaces show up?
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