Not done yet as of 2020! Will be done one day for sure.
Fabry Perot Interferometer by JFC UCL (2016)
Source. Description only, reasonable animations. Considers the case of two nearby beam splitters.Fabry-Perot Introduction by Williams College Physics (2020)
Source. Shows a working device. Confocal optical cavity, one of the mirrors scans back and forward moved by a piezoelectric motor, this is called a "scanning Fabry-Perot interferometer".
Does not produce an interference pattern, only an on/off blob, which is then fed into an oscilloscope for analysis. The oscilloscope shows both the mirror displacement (which is given by a voltage) and the light detector output.
The main FeathersJS hello world demo. Notable missing things...
- instant Heroku deployability: FeathersJS Heroku deployment
- no Front-end web framework which sucks, but there are basically official demos that worked e.g. feathers-chat-react
- FeathersJS signup email verification
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.
The Magnetic Moment of the Electron by Kusch and Foley (1948) by 
Ciro Santilli 35 Updated 2025-01-10 +Created 1970-01-01
Ciro Santilli 35 Updated 2025-01-10 +Created 1970-01-01Published on Physical Review by Polykarp Kusch and Foley.
journals.aps.org/pr/abstract/10.1103/PhysRev.74.250, paywall as of 2021.
Dumping examples under nodejs/sequelize/raw/many_to_many.js.
Not possible without subqueries in the standard syntax, a huge shame: stackoverflow.com/questions/1293330/how-can-i-do-an-update-statement-with-join-in-sql-server
GDM crashes sometimes when switching windows right after opening a new window: bugs.launchpad.net/ubuntu/+source/gdm/+bug/1956299
Spike.
Nucleocapsid phosphoprotein, sticks to the RNA inside.
www.nature.com/articles/s41467-020-20768-y mentions functions:
- helps pack the viral RNA into the capsule
- also has a side function in immune suppression
Dude took down a bank.
Good documentary about it: Nick Leeson and the Fall of the House of Barings by Adam Curtis (1996).
One is reminded of Annie Dookhan.
Bibliography review:
- Quantum Field Theory lecture notes by David Tong (2007) is the course basis
- quantum field theory in a nutshell by Anthony Zee (2010) is a good quick and dirty book to start
Course outline given:
- classical field theory
- quantum scalar field. Covers bosons, and is simpler to get intuition about.
- quantum Dirac field. Covers fermions
- interacting fields
- perturbation theory
- renormalization
Non-relativistic QFT is a limit of relativistic QFT, and can be used to describe for example condensed matter physics systems at very low temperature. But it is still very hard to make accurate measurements even in those experiments.
Defines "relativistic" as: "the Lagrangian is symmetric under the Poincaré group".
Mentions that "QFT is hard" because (a finite list follows???):But I guess that if you fully understand what that means precisely, QTF won't be too hard for you!
There are no nontrivial finite-dimensional unitary representations of the Poincaré group.
Notably, this is stark contrast with rotation symmetry groups (SO(3)) which appears in space rotations present in non-relativistic quantum mechanics.
www.youtube.com/watch?v=T58H6ofIOpE&t=5097 describes the relativistic particle in a box thought experiment with shrinking walls
- something about finding a unitary representation of the poincare group
- requires intense refrigeration to 15mK in dilution refrigerator. Note that this is much lower than the actual superconducting temperature of the metal, we have to go even lower to reduce noise enough, see e.g. youtu.be/uPw9nkJAwDY?t=471 from Video "Building a quantum computer with superconducting qubits by Daniel Sank (2019)"
- less connectivity, normally limited to 4 nearest neighbours, or maybe 6 for 3D approaches, e.g. compared to trapped ion quantum computers, where each trapped ion can be entangled with every other on the same chip
There are unlisted articles, also show them or only show them.