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IBB Blood Transfusion Packs is a 2012 red dot award: design concept winner.
With the IBB Blood Transfusion Packs there will be no room for error while administering blood to those who need it. The packaging makes it almost impossible for you to make a mistake, because the letters A, B, or O appear prominently when the bag is filled with blood. Every part of the bags except the letters is translucent and this is what makes it distinctive.
Needle playing a record | Victrola Coffee Roasters
Coloured scanning electron micrograph (SEM) of the needle (stylus) of a record player in a groove on a record. A record is used to store sound. It is produced by a machine with a head which vibrates in time to the sound being recorded. This cuts a groove in the record which varies according to the vibrations. A needle can then reproduce these vibrations as it runs along the groove and these, when amplified, produce the original sound.
Found Functions
“Nevertheless, the fact is that there is nothing as dreamy and poetic, nothing as radical, subversive, and psychedelic, as mathematics. It is every bit as mind blowing as cosmology or physics… and allows more freedom of expression than poetry, art, or music… Mathematics is the purest of the arts, as well as the most misunderstood.” - Paul Lockhart
Math is nature is math.
Math is the language of the universe
During a solar flare, magnetic field lines on the sun are often visible due to the flow of plasma—charged particles—along the lines. According to theory, these magnetic lines should remain intact, but they are sometimes observed breaking and reconnecting with other lines. An interdisciplinary team of researchers suggests that turbulence may be the missing link. In their magnetohydrodynamic simulation, they found that the presence of chaotic turbulent motions made the magnetic line motion entirely unpredictable, whereas laminar flows behaved according to conventional flux-freezing theory. (Photo credit: NASA SDO; Research credit: G. Eyink et al.; via SpaceRef; submitted by jshoer)
Druid. Prompt was “tree” I had a lot of fun working on a creature again! I don’t do it enough these days!
An interesting model of our solar system’s path as it travels through space in the Milky Way.
Certainly a departure from usual models that show the Sun as a static object, which it certainly isn’t
LIFE Science Book Covers, 1960s
Click on each image for details.
Neurons-in-the-brain by BWJones on Flickr.
From: prometheus.med.utah.edu/~bwjones/2013/02/this-is-your-bra…
Hemoglobin: Binding O2 — Cooperation Makes It Easier
I’m pretty sure I’m the only one in my biochemistry class that is so excited about how incredible the binding of oxygen to hemoglobin is that I’m losing sleep over it. Anyway, the gorgeous and colourful animination above, from the Research Collaboratory for Structural Bioinformatics Protein Data Bank (RCSB PDB), illustrates the conformational change upon oxygen binding to hemoglobin.
What is hemoglobin? Hemoglobin is a remarkable metalloprotein (a protein that contains a metal ion), found in red blood cells, that plays an important role in oxygen transport. Hemoglobin is a heterotetramer consisting of 2 α subunits (light pink and the other one can’t be seen) and 2 β subunits (light purple and light blue), arranged in 2 αβ subunits (2 sets of dimers). Each subunit contains one heme group (red) — a protoporphyrin ring with Fe2+ in the ring centre — resulting in four heme groups in total.2
How does hemoglobin bind O2? Interestingly, hemoglobin binds O2 (teal) cooperatively: when one heme group binds to O2, it increases the other heme groups’ affinity (ability to bind) for O2. This is a type of allosteric interaction — the change in shape of a protein that results from binding of a molecule at the allosteric site (a site other than the active site).2
Why does this happen? When O2 is not bound (deoxy), Fe2+ lies a little outside of the protoporphyrin ring. When O2 is bound (oxy), Fe2+ ”pops” into the ring, pulling with it a histidine (yellow), His, residue. Also attached to His is an α-helix (orange), which also shifts. All of this movement disrupts and forms new interactions between the α1β1-α2β2 interface.3 It is this conformational change that increases the other hemes’ ability to bind to O2. Noticeably, as more O2 binds to hemoglobin, the α1β1 dimer will rotate 15° relative to the α2β2 dimer, which can be observed in the animation.2
- Animations and movies illustrating conformational changes upon oxygen binding to hemoglobin (Janet Iwasa)
- YouTube video about hemoglobin-oxygen dynamics (ThePenguinProf)
- Ribbon structure of hemoglobin (The Full Wiki)
Sources used:
1. Hemoglobin animation: RCSB PDB
2. Krisinger, M. BIOC 202 Lecture on Protein Function. Presented at the University of British Columbia. May 27, 2013.
3. RCSB PDB. Hemoglobin. http://www.pdb.org/pdb/101/motm.do?momID=41 (accessed May 27, 2013)I’m glad I’m not the only one that thinks this is magnificent.
Image by Dr Jon Heras
An illustration of the progression of angiogenesis, which is the physiological process involving the growth of new blood vessels from pre-existing vessels. Tumours cannot grow beyond a few mm due to a lack of oxygen and other nutrients, so they encourage the formation of blood vessels to support their rapid cell division. For this reason, angiogenesis is a fundamental step in the transition of tumors from a dormant state to a malignant one.
