May K.

Seltene Sichtung: Was steckt hinter dem mysteriösen "Blauen Drachen"? Vor Mallorcas Küste hat eine Meeresbiologin den seltenen "Blauen Drachen" gesichtet. Was die Meeresschnecke so besonders macht und warum sie für Menschen ...

I just stumbled upon this incredibly artistic creature – the blue sea dragon – and couldn’t resist sharing its beauty with you. But don’t be fooled by its pretty looks – this #mollusc can deliver a painful sting!
www.geo.de/natur/tierwe...

Hannover offered brilliant crystallography but unfortunately, not crystal-clear air

I also couldn’t resist to stop by in the Wilhelm Busch Museum of Caricature and Drawings en.m.wikipedia.org/wiki/Wilhelm....

It was also a pleasure to attend the DGK conference dgk-conference.de in Hannover, meet so many impressive scientists, and hear inspiring talks.✨

A special week: 🎉Honored to receive the Waltrude & Friedrich Liebau Prize de.m.wikipedia.org/wiki/Liebau-Preis for promoting interdisciplinary crystallography with my ‘Protein Art’. I never dreamed my art would find its way into the hearts of distinguished scientists.

YouTube video by Veritasium The Most Useful Thing AI Has Ever Done

Great video by @veritasium.bsky.social on solving the 3D structure of proteins and how AI is revolutionizing the field!

youtube.com/watch?v=P_fH...

Here, RbAp46 has undergone its own transition – a carnivalistic one. And voilà – welcome the Cologne Fools’ Guild! #Cologne is one of the key cities for carnival celebrations, and today is #Rosenmontag – the peak of the festivities with grand parades and costumes.

Carnivalistic Protein Art

Protein: Histone chaperone RbAp46 (www.rcsb.org/structure/3cfs)
Drawing: Cologne Fools’ Guild

This protein helps to organize #histones, the spools around which DNA is wrapped, and regulates genes involved in cell growth and transition.

#Carnival #Cologne #ProteinArt

In the drawing, the crab is shown playing with bubbles instead of catching prey, reflecting ErbB4 in its inactive state. When the time comes, this crab will switch from resting to working, catching its ligand and triggering vital cellular messages. But for now, it’s just a crab at rest.

Interestingly, the word “cancer” comes from the Latin for “crab” because some tumors resemble crabs with their radiating “legs.” images.slideplayer.com/42/11199685/...

When ErbB4 functions correctly, it supports growth and differentiation in tissues like the mammary gland and nervous system. However, if ErbB4 gets mutated, it might misfire, contributing to cancer.

These stamps send signals below the surface to creatures like clams (representing the intracellular enzyme part, not shown here). The clams snap their shells shut, passing messages further underground to other residents, much like a kinase enzyme triggers signaling cascades inside the cell.

Imagine the receptor part as a hardworking crab perched on the surface of a cell. The whole crab represents the receptor parts of two ErbB4 proteins. Its “arms” reach out to catch specific activating molecules called ligands. When the crab catches its “prey,” it stamps on the sea ground.

Protein: #ErbB4 (www.rcsb.org/structure/2ahx)
Drawing: “A Crab at Rest”

The receptor tyrosine kinase ErbB4 is like a multi-module signal hub, consisting of a receptor and an enzyme. The receptor part receives signals, while the enzyme part sparks action inside the cell.

People with the most common form of late-onset Alzheimer’s often show elevated levels of BACE1. To highlight BACE1’s role in this disease, the enzyme is portrayed as an old man holding a leaky sack, with memories dripping away, capturing the heartbreaking loss of memory associated with Alzheimer’s.

One of the key mysteries of Alzheimer’s disease is the abnormal processing of a protein called amyloid β precursor protein (APP). BACE1, the protein featured in this drawing, is an enzyme that acts like molecular scissors, cutting APP in a way that contributes to the disease.

Age is the greatest risk factor, with approximately 5% of people aged 65–74 affected, and the probability rising to 13% for those in their next decade of life. This is a staggering figure, considering that it can strike anyone.

BACE1 in Alzheimer’s Disease

Drawing: “Worn out sack of memories”
Protein: #BACE1 (www.rcsb.org/structure/1SGZ)

#Alzheimer’s disease is a progressive brain disorder that slowly destroys memory, thinking skills, and the ability to carry out simple tasks.

Feet Taste Food — Biological Strategy — AskNature The feet of blowflies detect sugars via external taste receptors.

Fun fact: Did you know that #flies can taste sugar with their feet? Isn’t that a sweet connection?
asknature.org/strategy/fee...

To do this, it binds to a specialized receptor on the cell's surface. The "fly" in the drawing is inspired by the structure of an insulin dimer. Three of these dimers come together to form the inactive storage form of insulin, which is stabilized by a zinc ion.
upload.wikimedia.org/wikipedia/co...

The Insulin Fly

Protein: Insulin, www.rcsb.org/structure/3ir0

#Insulin is one of the best-known hormones that plays a key role in managing our metabolism. In its active form, a single insulin molecule (half of the "fly") helps to lower blood sugar levels by triggering cells to take up glucose.

exposing them to magnetic fields, bombarding them with electrons, or employing advanced computational efforts to model their shapes. Obtaining each three-dimensional structure is a monumental undertaking. Honoring these human achievements through art is nothing less than deserved!

Proteins truly are marvels of nature, and life without them unimaginable. It’s these intricate, functional forms of proteins that fascinate scientists. Researchers go to great lengths to study these structures — #crystallizing proteins for X-ray imaging,

Some function as messengers or couriers. Others spin like hamsters in a wheel to generate energy. There are even proteins with decorative roles — like #keratin, the key protein in our hair. Often, proteins team up to form large complexes, creating pumps or even motors.

— much like we use different tools for different tasks: sharp ones for cutting, needle-shaped for piercing, and hollow for scooping. Our protein toolbox is incredibly diverse. Some proteins act as tiny scissors, while others provide structural support, holding cells together like a frame.

Here’s where it gets exciting: the freshly assembled necklaces don’t stay flat. They immediately fold into complex three-dimensional structures. Each bead acts like a magnet, attracting or repelling others depending on its charge. This folding determines the protein’s function

These beads are then reassembled into new necklaces based on a precise instruction dictated by our DNA. Humans produce hundreds of thousands of different necklaces, each serving a unique purpose.

Surprisingly, our bodies aren’t fussy about the type of necklaces we eat. What matters is that they contain eight essential amino acids that we can’t produce ourselves. The remaining 12-13 amino acids are useful too, but if needed, our bodies can synthesize them.

Let’s take a closer look at what we’re actually consuming. A protein molecule can be imagined as a colorful bead necklace, with each bead representing an amino acid linked to others by a thread. During digestion, this necklace is broken into individual beads.

While not entirely wrong, as protein shakes and eggs indeed consist of proteins, this view is rather limited. Thinking of proteins only as food is as simplistic as seeing humans solely as eating machines.