Smparticle2 - Untitled

smparticle2 - Untitled
smparticle2 - Untitled
smparticle2 - Untitled
smparticle2 - Untitled
smparticle2 - Untitled
smparticle2 - Untitled
smparticle2 - Untitled
smparticle2 - Untitled

More Posts from Smparticle2 and Others

8 years ago
Novel Laminated Nanostructure Gives Steel Bone-like Resistance To Fracturing Under Repeated Stress

Novel laminated nanostructure gives steel bone-like resistance to fracturing under repeated stress

Metal fatigue can lead to abrupt and sometimes catastrophic failures in parts that undergo repeated loading, or stress. It’s a major cause of failure in structural components of everything from aircraft and spacecraft to bridges and powerplants. As a result, such structures are typically built with wide safety margins that add to costs.

Now, a team of researchers at MIT and in Japan and Germany has found a way to greatly reduce the effects of fatigue by incorporating a laminated nanostructure into the steel. The layered structuring gives the steel a kind of bone-like resilience, allowing it to deform without allowing the spread of microcracks that can lead to fatigue failure.

The findings are described in a paper in the journal Science by C. Cem Tasan, the Thomas B. King Career Development Professor of Metallurgy at MIT; Meimei Wang, a postdoc in his group; and six others at Kyushu University in Japan and the Max Planck Institute in Germany.

“Loads on structural components tend to be cyclic,” Tasan says. For example, an airplane goes through repeated pressurization changes during every flight, and components of many devices repeatedly expand and contract due to heating and cooling cycles. While such effects typically are far below the kinds of loads that would cause metals to change shape permanently or fail immediately, they can cause the formation of microcracks, which over repeated cycles of stress spread a bit further and wider, ultimately creating enough of a weak area that the whole piece can fracture suddenly.

Read more.


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7 years ago

The Six Types of Middle-Earth Names

1. Characters whose Names are Secretly Insults: 

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Samwise: means “Half-wise” or “Half-wit.” He is Stupid Gamgee

Faramir: Boromir’s name means “steadfast jewel”, but Faramir’s name just means “sufficient jewel.”

Sufficient.

Denethor took one look at baby Faramir and thought “eh I guess he exists or whatever” which is very in character

 2. Characters who Have Way Too Many Names

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Examples include Aragorn son of Arathorn son of Arador heir of Isildur Elendil’s son, descendant of Numenor,  Thorongill,  Eagle of the Star,  Dúnadan, Strider,  Wingfoot, Longshanks, Elessar, Edhelharn, Elfstone, Estel (”Hope,”) The Chieftain of the Dúnedain, King of the West, High King of Gondor and Arnor, and Envinyatar the Renewer of the House of Telcontar

Wait I’m sorry did I say “examples” plural Cuz that was all one guy 3. Characters whose parents must’ve been prophets

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-Frodo means “wise by experience.” His story is about becoming wise by experience -A lady named Elwing turns into a bird (geddit)

4. Characters whose families were so lazy that they copy-pasted the same first half of a name onto multiple people

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Théoden/Théodred  Aragorn/Arathorn/Arador  Éomer/ Éomund/Éowyn/Éorl Elladan/Elrohir/Elrond/Elros/Elwing/Elenwë/Elendil/Eldarion (the laziest family) 

5.Characters whose Names are Expertly Designed so that Newbies can’t Remember Who is Who and Feel Sad

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All the people mentioned in number 4 Celeborn, Celegorm, Celebrimbor, Celebrian All the rhyming dwarf names in the Hobbit Sauron and Saruman Arwen and Éowyn

6. Name so nice, you say it twice

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Legoas Greenleaf: Legolas’s first name means “Greenleaf” in elvish. Legolas is Greenleaf Greenleaf (thranduil really likes green leaves ok) King Théoden’s name means King in Rohirric. Tolkien decided to name his king “King.” All hail King King  this is what the fanbase means when we say tolkien was a creative genius with language

8 years ago

Stress raisers!

The De Havilland DH 106 Comet In Flight, The Worlds First Commercial Jetliner. 1952-1953

The de Havilland DH 106 Comet in flight, the worlds first commercial jetliner. 1952-1953

via reddit

Keep reading

8 years ago
“I Travel Around The World, Eat A Lot Of Shit, And Basically Do Whatever The Fuck I Want.”  Read

“I travel around the world, eat a lot of shit, and basically do whatever the fuck I want.”  Read our complete Profile of Anthony Bourdain here. 

7 years ago
You Are The Center Of Wonderland & Keep The Last Glow In Mind By Jana Luo
You Are The Center Of Wonderland & Keep The Last Glow In Mind By Jana Luo

You are the center of wonderland & Keep the last glow in mind by Jana Luo

8 years ago
“It Is The Most Passionate Relationship Of The Film. It Is Almost Equivalent To That Of Scarlett O’hara
“It Is The Most Passionate Relationship Of The Film. It Is Almost Equivalent To That Of Scarlett O’hara

“It is the most passionate relationship of the film. It is almost equivalent to that of Scarlett O’hara and Ashley Wilkes and Scarlett and Rhett Butler. Mammy is Scarlett’s true mother. It is Mammy to whom Scarlett goes to for advice, it is Mammy who sees deeply into Scarlett’s emotions and knows everything that’s going on with her. Whereas Scarlett’s biological mother doesn’t understand the emotional turmoil of her daughter. This is an incredible performance, very inflictive, that unfortunately is never getting discussed these days because of the sensitivity we should properly feel.” -Camille Paglia

8 years ago
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by: Jannik Obenhoff

8 years ago
(Image Caption: Brain Showing Hallmarks Of Alzheimer’s Disease (plaques In Blue). Credit: ZEISS Microscopy)

(Image caption: Brain showing hallmarks of Alzheimer’s disease (plaques in blue). Credit: ZEISS Microscopy)

New imaging technique measures toxicity of proteins associated with Alzheimer’s and Parkinson’s diseases

Researchers have developed a new imaging technique that makes it possible to study why proteins associated with Alzheimer’s and Parkinson’s diseases may go from harmless to toxic. The technique uses a technology called multi-dimensional super-resolution imaging that makes it possible to observe changes in the surfaces of individual protein molecules as they clump together. The tool may allow researchers to pinpoint how proteins misfold and eventually become toxic to nerve cells in the brain, which could aid in the development of treatments for these devastating diseases.

The researchers, from the University of Cambridge, have studied how a phenomenon called hydrophobicity (lack of affinity for water) in the proteins amyloid-beta and alpha synuclein – which are associated with Alzheimer’s and Parkinson’s respectively – changes as they stick together. It had been hypothesised that there was a link between the hydrophobicity and toxicity of these proteins, but this is the first time it has been possible to image hydrophobicity at such high resolution. Details are reported in the journal Nature Communications.

“These proteins start out in a relatively harmless form, but when they clump together, something important changes,” said Dr Steven Lee from Cambridge’s Department of Chemistry, the study’s senior author. “But using conventional imaging techniques, it hasn’t been possible to see what’s going on at the molecular level.”

In neurodegenerative diseases such as Alzheimer’s and Parkinson’s, naturally-occurring proteins fold into the wrong shape and clump together into filament-like structures known as amyloid fibrils and smaller, highly toxic clusters known as oligomers which are thought to damage or kill neurons, however the exact mechanism remains unknown.

For the past two decades, researchers have been attempting to develop treatments which stop the proliferation of these clusters in the brain, but before any such treatment can be developed, there first needs to be a precise understanding of how oligomers form and why.

“There’s something special about oligomers, and we want to know what it is,” said Lee. “We’ve developed new tools that will help us answer these questions.”

When using conventional microscopy techniques, physics makes it impossible to zoom in past a certain point. Essentially, there is an innate blurriness to light, so anything below a certain size will appear as a blurry blob when viewed through an optical microscope, simply because light waves spread when they are focused on such a tiny spot. Amyloid fibrils and oligomers are smaller than this limit so it’s very difficult to directly visualise what is going on.

However, new super-resolution techniques, which are 10 to 20 times better than optical microscopes, have allowed researchers to get around these limitations and view biological and chemical processes at the nanoscale.

Lee and his colleagues have taken super-resolution techniques one step further, and are now able to not only determine the location of a molecule, but also the environmental properties of single molecules simultaneously.

Using their technique, known as sPAINT (spectrally-resolved points accumulation for imaging in nanoscale topography), the researchers used a dye molecule to map the hydrophobicity of amyloid fibrils and oligomers implicated in neurodegenerative diseases. The sPAINT technique is easy to implement, only requiring the addition of a single transmission diffraction gradient onto a super-resolution microscope. According to the researchers, the ability to map hydrophobicity at the nanoscale could be used to understand other biological processes in future.


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