The Mistress of Metal

This is a social experiment. Won't you join me?

xsugartownx:

"Dear brothers and sisters, do remember one thing: Malala Day is not my day. Today is the day of every woman, every boy and every girl who have raised their voice for their rights.

Dear Friends, on the 9th of October 2012, the Taliban shot me on the left side of my forehead. They shot my friends too. They thought that the bullets would silence us. But they failed. The terrorists thought that they would change our aims and stop our ambitions, but nothing changed in my life except this: weakness, fear and hopelessness died. Strength, power and courage was born.  I am the same Malala. My ambitions are the same. My hopes are the same. My dreams are the same.

The wise saying ‘the pen is mightier than sword’ was true. The extremists are afraid of books and pens. The power of education frightens them. They are afraid of women. The power of the voice of women frightens them. Through hate-filled actions, extremists have shown what frightens them the most: a girl with a book.

Peace is necessary for education. In many parts of the world, terrorism, wars and conflicts stop children to go to their schools. We are really tired of these wars. There was a time when women social activists asked men to stand up for their rights. But, this time, we will do it by ourselves. I am not telling men to step away from speaking for women’s rights. Rather, I am focusing on women to be independent to fight for themselves. 

Today we call upon all communities to be tolerant – to reject prejudice based on caste, creed, sect, religion or gender. We cannot all succeed when half of us are held back.

We call upon our sisters around the world to be brave – to embrace the strength within themselves and realise their full potential. 

Let us pick up our books and pens. They are our most powerful weapons. 

We must not forget that our sisters and brothers are waiting for a bright peaceful future.”

And with that I’m up and going to write.

(via theskyyends)

spaceplasma:

Kickstarter plasma thruster could launch nano-satellites for cheap

A Kickstarter project is attempting to raise funds for a plasma thruster that will propel mini satellites into deep space for a 1/1,000th of the cost of previous missions.
The CAT plasma thruster will be able to push 5kg nanosatellites called CubeSats far beyond Earth’s orbit. Before the system is ready to propel satellites into deep space, it will first need to be tested on the ground and within these Earth’s orbit. If enough funding is secured, two spacecraft will be launched into interplanetary space.
Usually CubeSats piggyback on larger rockets, drift around the Earth, trapped in their original orbit until they eventually de-orbit and burn up in the Earth’s atmosphere. The idea is to send the little satellites much deeper in space, and use them for a variety of different purposes, including searching for life, gathering data about solar flares and the aurora, inspecting asteroids. They could also be used as network nodes to provide cheap global internet access, more current satellite photos and better global weather observations. The engineers behind the project have even suggested they might be able to create an interplanetary internet.
The minimum donation is $5 (£3.32), but if you’re hoping to get your name etched on a spacecraft panel, like an “interplanetary message in a bottle”, you’ll need to cough up a minimum of $60 (£39.81). If being part of a grand exploratory space mission with your name plastered on the side isn’t quite personalised enough for you, there’s  another Kickstarter project looking for funding at the moment that allows you design and launch your own tiny spacecraft.
The project is being run by the University of Michigan’s Aerospace Engineering department working in collaboration with several NASA research centres, and at the time of writing, the has raised $1,120 (£743) of its $200,000 (£133,000) target. If you want to donate, head over to  its Kickstarter page by 5 August.


Credit: Katie Collins/wired.co.uk

Also #science.

spaceplasma:

Kickstarter plasma thruster could launch nano-satellites for cheap

A Kickstarter project is attempting to raise funds for a plasma thruster that will propel mini satellites into deep space for a 1/1,000th of the cost of previous missions.

The CAT plasma thruster will be able to push 5kg nanosatellites called CubeSats far beyond Earth’s orbit. Before the system is ready to propel satellites into deep space, it will first need to be tested on the ground and within these Earth’s orbit. If enough funding is secured, two spacecraft will be launched into interplanetary space.

Usually CubeSats piggyback on larger rockets, drift around the Earth, trapped in their original orbit until they eventually de-orbit and burn up in the Earth’s atmosphere. The idea is to send the little satellites much deeper in space, and use them for a variety of different purposes, including searching for life, gathering data about solar flares and the aurora, inspecting asteroids. They could also be used as network nodes to provide cheap global internet access, more current satellite photos and better global weather observations. The engineers behind the project have even suggested they might be able to create an interplanetary internet.

The minimum donation is $5 (£3.32), but if you’re hoping to get your name etched on a spacecraft panel, like an “interplanetary message in a bottle”, you’ll need to cough up a minimum of $60 (£39.81). If being part of a grand exploratory space mission with your name plastered on the side isn’t quite personalised enough for you, there’s another Kickstarter project looking for funding at the moment that allows you design and launch your own tiny spacecraft.

The project is being run by the University of Michigan’s Aerospace Engineering department working in collaboration with several NASA research centres, and at the time of writing, the has raised $1,120 (£743) of its $200,000 (£133,000) target. If you want to donate, head over to its Kickstarter page by 5 August.

Credit: Katie Collins/wired.co.uk

Also #science.

(via crookedindifference)

itsreallylate:

hockeyteeth:

hockeyteeth:

This is Steven. He’s my best friend. We’re going on 6 years together now, and I couldn’t imagine my life without such an awesome person. He was extremely healthy, and the only time I ever had to take him to the hospital was when he stage-dove during a set of a band he didn’t even really like, and the crowd moved, which made him fall on the ground and crack his arm in half. Good times. ANYWAYS, like I was saying, super healthy guy, right?

Right around December 1st, he started feeling kind of sick. His stomach was bothering him, but we figured he just ate something spicy or something didn’t agree with him, etc. Two weeks later it wasn’t going away, and he finally gave me the details of the situation, so I made him go to the doctor. Doctor transferred him to a GI (gastrointestinal) specialist, which of course took FOREVER, so on Christmas Eve when he decided he couldn’t handle the pain anymore, I skipped my family trip to grandma’s house and we took a trip to the urgent care instead, where they prescribed him some antibiotics and steroids and sent him on his way. By this time he had lost about 30lbs. While all of this was going on, he wasn’t eating, because everything he ate went straight through him and he wasn’t gaining any nutrition. I’ll save you the gory details, but just know he was also losing a ton of blood every time he used the restroom. He was pale, super skinny, extremely dehydrated and he looked like a completely different person.

We somehow made it through Christmas, and on New Years Eve, he had his colonoscopy. This was going to tell us everything that was wrong and it was going to be fixed and done with. Or that’s what was supposed to happen, anyways. He had his colonscopy, and the doctor diagnosed him with Ulcerative Colitis - the worst case he’s ever seen. I need to add here that they also biopsied his colon about 8 times to check for cancers. That’s important because that’s the reason his colon tore open a week later. 

He was at home not getting any better, and one night he had extreme pain in his side. He though his appendix had burst, so he called his parents phone. Both of them had their phones turned off. He called me but my phone was on silent. Thankfully, his little brother answered. That is a miracle in itself for reasons I won’t bore you with, but let’s just say his brother is a heavy, HEAVY sleeper, and he doesn’t remember that phone call. His parents rushed him to the ER and he was taken into surgery immediately.

I woke up the next morning not having a clue what was going because my stupid phone was on silent for WHO KNOWS WHAT REASON. It’s never on silent and I still can’t believe that happened. I had about 40 missed calls from Steven and his parents and a ton of texts asking me if I was okay. I called to find out he was taken into surgery and they didn’t know how bad it was. They didn’t even know what was going to happen to him. 

After a major panic attack, I rushed to the hospital to find out he was coming out of surgery and that they had removed 90% of his colon. Listen, you need your colon. It forms your stool and makes it hard, and it soaks up all your water and minerals. Without it, life is tough.

Not only was his colon pretty much gone, but all of the bacteria and stool that was in there was now in his bloodstream and he went septic. He was placed in the ICU for three days and then transferred to a regular room. His incision wasn’t healing, so about 2 weeks into his hospital stay they took out all of his staples on his stomach, leaving a literal 3” wide x 7” long x 3” deep gaping hole to do this thing called “wet-dry” packs, where they dip gauze in saline, shove it in the wound, let it dry, and then rip it out, pulling out all the bacteria. They did this three times a day for about a week, until they realized it wasn’t working. That’s something I could barely handle watching. I’ve never seen someone in so much pain.

Somewhere in there his lung collapsed, they had to put a tube in his side and drain fluid, and then they couldn’t get his fever down the entire month he was there so they inserted a PICC line to administer antibiotics straight to his heart. Also throw in a persistent rash, drains on both sides of his pelvis that gave us nothing but problems, and so many other health issues.  

To heal his incision they sent him home with a Wound-Vac which is like a space bag on your wound, constantly sucking out bacteria. He was hospitalized for a month, and then on home health care for a month where we administered his antibiotics by IV and a nurse came and changed his dressing every Monday, Wednesday, and Friday. He had lost a total of 60 lbs, and as you can see from the pictures, he was extremely skinny.

We’re just now getting back to normal, and he has surgery again June 10 to form a mock-colon called a J-pouch. Modern medicine is incredible.

His mom, who was the one in the family with the insurance, lost her job while Steven was in the hospital.

Yeah, no more insurance. His parents are also about to lose their house due to her losing her job.

Now that you know Steven’s story, if you have the means to donate a little, I can’t stress how much it would help us. Our lives are put on hold and we can’t move forward until we figure out how in the world we’re going to pay for these medical bills. Although the emergency surgery is over, he still has at least two more coming up, and the bills are looming. The price of medical supplies and hospital stays are the biggest scam, and I don’t know how we are going to make this work. If you aren’t able, all I ask is that you would kindly repost this so that maybe someone will hear his story. I am so happy to say that he is alive and on track to being healthy, and although he may never be 100% back to his “normal” self, he made it through everything and he’s alive and that’s enough to be thankful for in itself. 

If you would like to donate, you can do so here: 

https://www.paypal.com/cgi-bin/webscr?cmd=_donations&business=6DAWCNVVRQVMG&lc=US&item_name=Steven%27s%20Surgery%20Fund&currency_code=USD&bn=PP%2dDonationsBF%3abtn_donate_LG%2egif%3aNonHosted

250 notes on this! I can’t believe how much support I’ve gotten from Tumblr. We made it halfway to our goal in a single day. People like you guys give me so much faith in humanity. This is a big deal to me personally because I see the direct change in Steven already. He doesn’t have a tumblr, but he wanted me to say thank you. Thank you SO much. I’ve cried so many times over donations and blessings from people I may or may not know. This is so overwhelming. 

We’re halfway to our goal, so if you can’t donate, I totally understand that! Money sucks. TRUST ME, we know…but reblogging still helps! Thank you all so much for your generosity. 

REBLOG PLEASE!

As someone staring a shitton of medical bills in the face that I can’t pay, help this guy, we are one. #onelove

(via theskyyends)

neurosciencestuff:

Researchers Design Variant of Main Painkiller Receptor 
Opioids, such as morphine, are still the most effective class of painkillers, but they come with unwanted side effects and can also be addictive and deadly at high doses. Designing new pain-killing drugs of this type involves testing them on their corresponding receptors, but access to meaningful quantities of these receptors that can work in experimental conditions has always been a limiting factor. 
Now, an interdisciplinary collaboration between researchers at the University of Pennsylvania has developed a variant of the mu opioid receptor that has several advantages when it comes to experimentation. This variant can be grown in large quantities in bacteria and is also water-soluble, enabling experiments and applications that had previously been very challenging or impossible.  
The study was led by Renyu Liu, an assistant professor in the Department of Anesthesiology and Critical Care at Penn’s Perelman School of Medicine, and Jeffery Saven, an associate professor in the Department of Chemistry in the School of Arts and Sciences. Jose Manuel Perez-Aguilar, then a graduate student in the Department of Chemistry, and Jin Xi, Felipe Matsunaga and Xu Cui, lab members in the Department of Anesthesiology and Critical Care, along with Bernard Selling of Impact Biologicals Inc., contributed significantly to this study.
Their research was published in the Journal PLOS ONE.
The mu opioid receptor belongs to a class of cellular membrane proteins called G protein-coupled receptors, or GPCRs. Involved in wide range of biological processes, these receptors bind to molecules in the environment, initiating cellular signaling pathways. In the case of this receptor, binding to opioid molecules leads to a profound reduction of pain but also to a variety of unpleasant and potentially fatal side-effects, a problem that researchers from multiple disciplines are attempting to address.
“There are two directions for solving this problem in basic science, either working on the opioid molecule or working on the receptor,” Liu said. “We’re doing the latter.”
Experimenting on the mu opioid receptor has been challenging for several reasons. The human receptor itself is relatively scarce, appearing in small quantities on only a few types of cells, making harvesting appreciable amounts impractical. Researchers have also been unable to grow it recombinantly — genetically engineering bacteria to express the protein en masse — as some parts of the protein are toxic to E.coli. Hydrophobic, or water-hating, amino acid groups on the exterior of the receptor that help it sit in the cell’s membrane also make it insoluble in water when isolated.
The researchers set out to address these challenges by computationally designing variants of the mu opioid receptor. This task had challenges of its own; their research was conducted long before the crystal structure of receptor was known.         
“The problem with this receptor is that the native structure has only very recently been solved and only a significant re-engineered mouse model at that,” Liu said. “When we started this project, we were blind.”
Starting with only the gene sequence for the human version of the receptor, the researchers knew the order of the protein’s amino acids but not how they were folded together. The structures for other GPCRs, such as rhodopsin and the beta-2 adrenergic receptor, were known at the time, however.
“Based on the comparison of our sequence to the sequences of those GPCRs, we built a computer model of the protein,” Saven said. “When the structure of the mouse version of this receptor appeared, we were able to compare our model to that structure, and they matched up really well.”
From that comparison, the researchers were able to identify the hydrophobic amino acids on the exterior of the structure, as well as some of those that were potentially toxic to E. coli.
“The objective then was to redesign those exterior amino acids,” Saven said. “Based on the physical and chemical interactions these amino acids have with each other and with water, we were able to identify sequence combinations that are consistent with the model — where atoms don’t overlap in space — and preferentially occupy the exterior surface with ones that are water soluble.”
Replacing 53 of the protein’s 288 amino acids, the research team introduced the new gene sequence into E. coli, which were able to produce large quantities of the variant. Beyond looking like the now-available mouse mu opioid receptor, the researchers were able to show its value to future studies by performing functional tests.  
“We showed that this water-soluble form of the protein can compete with the native, membrane-based form when binding with antagonists that are fluorescently labeled,” Saven said. “You can watch the fluorescence shift as more of these water-soluble variants are floating around in the solution.”   
The team’s computational approach enables further iterations of the variant to be more easily designed, meaning it can be tweaked alongside experimental conditions. 
“This is a great product that can do a lot of things,” Liu said. “You can use this variant to look at the structure-function relationship for the receptor, or even potentially use it as a screening tool.”

Neurotic. ;)

neurosciencestuff:

Researchers Design Variant of Main Painkiller Receptor

Opioids, such as morphine, are still the most effective class of painkillers, but they come with unwanted side effects and can also be addictive and deadly at high doses. Designing new pain-killing drugs of this type involves testing them on their corresponding receptors, but access to meaningful quantities of these receptors that can work in experimental conditions has always been a limiting factor. 

Now, an interdisciplinary collaboration between researchers at the University of Pennsylvania has developed a variant of the mu opioid receptor that has several advantages when it comes to experimentation. This variant can be grown in large quantities in bacteria and is also water-soluble, enabling experiments and applications that had previously been very challenging or impossible.  

The study was led by Renyu Liu, an assistant professor in the Department of Anesthesiology and Critical Care at Penn’s Perelman School of Medicine, and Jeffery Saven, an associate professor in the Department of Chemistry in the School of Arts and Sciences. Jose Manuel Perez-Aguilar, then a graduate student in the Department of Chemistry, and Jin Xi, Felipe Matsunaga and Xu Cui, lab members in the Department of Anesthesiology and Critical Care, along with Bernard Selling of Impact Biologicals Inc., contributed significantly to this study.

Their research was published in the Journal PLOS ONE.

The mu opioid receptor belongs to a class of cellular membrane proteins called G protein-coupled receptors, or GPCRs. Involved in wide range of biological processes, these receptors bind to molecules in the environment, initiating cellular signaling pathways. In the case of this receptor, binding to opioid molecules leads to a profound reduction of pain but also to a variety of unpleasant and potentially fatal side-effects, a problem that researchers from multiple disciplines are attempting to address.

“There are two directions for solving this problem in basic science, either working on the opioid molecule or working on the receptor,” Liu said. “We’re doing the latter.”

Experimenting on the mu opioid receptor has been challenging for several reasons. The human receptor itself is relatively scarce, appearing in small quantities on only a few types of cells, making harvesting appreciable amounts impractical. Researchers have also been unable to grow it recombinantly — genetically engineering bacteria to express the protein en masse — as some parts of the protein are toxic to E.coli. Hydrophobic, or water-hating, amino acid groups on the exterior of the receptor that help it sit in the cell’s membrane also make it insoluble in water when isolated.

The researchers set out to address these challenges by computationally designing variants of the mu opioid receptor. This task had challenges of its own; their research was conducted long before the crystal structure of receptor was known.         

“The problem with this receptor is that the native structure has only very recently been solved and only a significant re-engineered mouse model at that,” Liu said. “When we started this project, we were blind.”

Starting with only the gene sequence for the human version of the receptor, the researchers knew the order of the protein’s amino acids but not how they were folded together. The structures for other GPCRs, such as rhodopsin and the beta-2 adrenergic receptor, were known at the time, however.

“Based on the comparison of our sequence to the sequences of those GPCRs, we built a computer model of the protein,” Saven said. “When the structure of the mouse version of this receptor appeared, we were able to compare our model to that structure, and they matched up really well.”

From that comparison, the researchers were able to identify the hydrophobic amino acids on the exterior of the structure, as well as some of those that were potentially toxic to E. coli.

“The objective then was to redesign those exterior amino acids,” Saven said. “Based on the physical and chemical interactions these amino acids have with each other and with water, we were able to identify sequence combinations that are consistent with the model — where atoms don’t overlap in space — and preferentially occupy the exterior surface with ones that are water soluble.”

Replacing 53 of the protein’s 288 amino acids, the research team introduced the new gene sequence into E. coli, which were able to produce large quantities of the variant. Beyond looking like the now-available mouse mu opioid receptor, the researchers were able to show its value to future studies by performing functional tests.  

“We showed that this water-soluble form of the protein can compete with the native, membrane-based form when binding with antagonists that are fluorescently labeled,” Saven said. “You can watch the fluorescence shift as more of these water-soluble variants are floating around in the solution.”   

The team’s computational approach enables further iterations of the variant to be more easily designed, meaning it can be tweaked alongside experimental conditions. 

“This is a great product that can do a lot of things,” Liu said. “You can use this variant to look at the structure-function relationship for the receptor, or even potentially use it as a screening tool.”

Neurotic. ;)

thenewenlightenmentage:

How Do Planets Form?

According to our current understanding, a star and its planets form out of a collapsing cloud of dust and gas within a larger cloud called a nebula. As gravity pulls material in the collapsing cloud closer together, the center of the cloud gets more and more compressed and, in turn, gets hotter. This dense, hot core becomes the kernel of a new star.1

This model is called the Solar Nebular Disk Model.  This model is challenged by accretion models.

The prevailing model for planetary accretion, also called fractal assembly, and dating back as far as the 18th century, assumes that the Solar System’s planets grew as small grains colliding chaotically, coalescing into bigger ones, colliding yet more until they formed planetesimals. The planetesimals then collided until they formed planets as varied as the Earth and Jupiter.2

This model fits well with the formation of Earth’s moon as well.

According to the Giant Impact Theory, proposed in its modern form at a conference in 1975, Earth’s moon was created in an apocalyptic collision between a planetary body called Theia (in Greek mythology the mother of the moon Selene) and the early Earth.
This collision was so powerful it is hard for mere mortals to imagine, but the asteroid that killed the dinosaurs is thought to have been the size of Manhattan, whereas Theia is thought to have been the size of the planet Mars.
The smashup released so much energy it melted and vaporized Theia and much of the proto-Earth’s mantle. The Moon then condensed out of the cloud of rock vapor, some of which also re-accreted to the Earth.3

Accretion models are generally accepted when speaking of moon formation, ring formation and even the formation of black holes. However, in the case of ring formation, some rings form because their planet cannot accrete the material; this is considered true in Saturn’s case.4
So, have these models been observed?  Indeed!  The most recent case is the formation of a planet around the star TW Hydrae. 

The finding may change the current planet formation theories!5
Another well known case is that of Formalhaut b.  Is it there, is it not there ?  Please read that question in your coolest Scottish accent!

The planet actually follows a rather strange elliptical orbit; it swings as close as 4.6 billion miles to its star and as far as 27 billion miles from its star.6  Some kinda lasso you got ther partner!
1 http://hubblesite.org/hubble_discoveries/discovering_planets_beyond/how-do-planets-form
2 http://www.astrobio.net/pressrelease/4602/a-new-model-for-planet-formation
3 http://phys.org/news/2012-10-massive-planetary-collision-zapped-key.html
4 http://www.universetoday.com/84129/why-does-saturn-have-rings/
5 http://www.nasa.gov/mission_pages/hubble/science/tw-hydrae.html
6 http://www.nasa.gov/mission_pages/hubble/science/rogue-fomalhaut.html
GIF Courtesy: Watch Here

thenewenlightenmentage:

How Do Planets Form?

According to our current understanding, a star and its planets form out of a collapsing cloud of dust and gas within a larger cloud called a nebula. As gravity pulls material in the collapsing cloud closer together, the center of the cloud gets more and more compressed and, in turn, gets hotter. This dense, hot core becomes the kernel of a new star.1

This model is called the Solar Nebular Disk Model.  This model is challenged by accretion models.

The prevailing model for planetary accretion, also called fractal assembly, and dating back as far as the 18th century, assumes that the Solar System’s planets grew as small grains colliding chaotically, coalescing into bigger ones, colliding yet more until they formed planetesimals. The planetesimals then collided until they formed planets as varied as the Earth and Jupiter.2

This model fits well with the formation of Earth’s moon as well.

According to the Giant Impact Theory, proposed in its modern form at a conference in 1975, Earth’s moon was created in an apocalyptic collision between a planetary body called Theia (in Greek mythology the mother of the moon Selene) and the .

This collision was so powerful it is hard for mere mortals to imagine, but the asteroid that killed the dinosaurs is thought to have been the size of Manhattan, whereas Theia is thought to have been the size of the planet Mars.

The smashup released so much energy it melted and vaporized Theia and much of the proto-Earth’s mantle. The Moon then condensed out of the cloud of rock vapor, some of which also re-accreted to the Earth.3

Accretion models are generally accepted when speaking of moon formation, ring formation and even the formation of black holes. However, in the case of ring formation, some rings form because their planet cannot accrete the material; this is considered true in Saturn’s case.4

So, have these models been observed?  Indeed!  The most recent case is the formation of a planet around the star TW Hydrae. 

The finding may change the current planet formation theories!5

Another well known case is that of Formalhaut b.  Is it there, is it not there ?  Please read that question in your coolest Scottish accent!

The planet actually follows a rather strange elliptical orbit; it swings as close as 4.6 billion miles to its star and as far as 27 billion miles from its star.6  Some kinda lasso you got ther partner!

http://hubblesite.org/hubble_discoveries/discovering_planets_beyond/how-do-planets-form

http://www.astrobio.net/pressrelease/4602/a-new-model-for-planet-formation

http://phys.org/news/2012-10-massive-planetary-collision-zapped-key.html

http://www.universetoday.com/84129/why-does-saturn-have-rings/

http://www.nasa.gov/mission_pages/hubble/science/tw-hydrae.html

http://www.nasa.gov/mission_pages/hubble/science/rogue-fomalhaut.html

GIF Courtesy: Watch Here

thedailyshow:

“Welcome to The Daily Show, I am John Oliver. And let’s just acknowledge for a moment that this is weird. This looks weird. It feels weird. It even sounds weird. It sounds weird to me and this is my actual voice.” - John Oliver http://on.cc.com/1707klp

Jon oliver takes over the daily show.

thedailyshow:

“Welcome to The Daily Show, I am John Oliver. And let’s just acknowledge for a moment that this is weird. This looks weird. It feels weird. It even sounds weird. It sounds weird to me and this is my actual voice.” - John Oliver http://on.cc.com/1707klp

Jon oliver takes over the daily show.