- 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 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.
Parent/predecessor of ASML.
The degree of some algebraic structure is some parameter that describes the structure. There is no universal definition valid for all structures, it is a per structure type thing.
This is particularly useful when talking about structures with an infinite number of elements, but it is sometimes also used for finite structures.
Examples:
- the dihedral group of degree n acts on n elements, and has order 2n
- the parameter that characterizes the size of the general linear group is called the degree of that group, i.e. the dimension of the underlying matrices
en.wikipedia.org/wiki/Paulo_Freire:OMG so nice.
During his childhood and adolescence, Freire ended up four grades behind, and his social life revolved around playing pick-up football with other poor children, from whom he claims to have learned a great deal. These experiences would shape his concerns for the poor and would help to construct his particular educational viewpoint. Freire stated that poverty and hunger severely affected his ability to learn. These experiences influenced his decision to dedicate his life to improving the lives of the poor: "I didn't understand anything because of my hunger. I wasn't dumb. It wasn't lack of interest. My social condition didn't allow me to have an education. Experience showed me once again the relationship between social class and knowledge"
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