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Message boards : News : New publication: Our study of a disordered protein and its significance

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Profile nate
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Message 38742 - Posted: 29 Oct 2014 | 13:04:31 UTC

Hi everyone,

We are very pleased to announce the publication of our latest research article, titled "Kinetic modulation of a disordered protein domain by phosphorylation", which was published yesterday in the journal Nature Communications. You can see the official journal page link here. Since we know most of you don't have access to the fancy formatted version from Nature Publishing Group, we have placed the our less-fancy formatted pre-print version of the article here (first PDF link at the top of the page).

Since I am sure the title and abstract is quite cryptic/confusing to everyone, let me explain what we discovered and why this work was important. The main focus of the paper was a disordered protein domain called KID. Disordered proteins like KID do not have any rigid structures (so no x-ray crystal structures), and are in fact very flexible like polymers. However, despite being flexible they are very important and common in many different aspects of cell biology. They are important in many protein-protein interactions, such as ones that are important in communication inside the cell. They are frequently involved in many diseases like cancer (among many others).

KID is a protein that has been studied for more than 15 years, and a lot was already known about it. Other proteins in the cell chemically modify KID through a process known as phosphorylation, which then causes it to bind to specific proteins. It binds most famously to a protein known as KIX. The behavior of KID in the phosphorylated and normal state has been studied by a technique known as NMR (a cousin of MRI), and the binding of KID to KIX has also been studied this way. However, what we discovered in our study—and not seen by any other method yet—was that when KID is phosphorylated, it undergoes an a slowdown in its motions and forms a temporary, partially folded state. We believe this state is important in the binding process, and modelling and comparison with previous experiments also suggest this. This work is significant because it is the first time anyone has shown that such chemical modifications could change the behavior of a protein in this way, and also that it could have important consequences for the way proteins interact.

If you have questions, please ask away. We will assign badges and update the webpage soon.

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Message 38749 - Posted: 29 Oct 2014 | 15:49:05 UTC

Badges updated! (Thanks to Toni)

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Message 38757 - Posted: 29 Oct 2014 | 20:46:47 UTC
Last modified: 29 Oct 2014 | 20:49:27 UTC

Nature Communications - wow, congratulations guys! And scientifically this sounds like an important leap forward :)

BTW: shouldn't you get a super badge for your own paper, nate?

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Message 38758 - Posted: 29 Oct 2014 | 20:52:09 UTC - in response to Message 38749.

Substantive work. Your solid comparison to the NMR model is critical to further establishing and defining in Silico modelling as an acceptable if not superior alternative to the often more expensive, more invasive, more limited and less safe in vitro and in vivo research methodologies.
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Message 38764 - Posted: 30 Oct 2014 | 1:25:27 UTC - in response to Message 38742.

Strong work, Nate! This is my first publication on GPUGrid too, yay!

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Message 38765 - Posted: 30 Oct 2014 | 4:05:41 UTC

Congratulations for the publication and the achieved results.

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Message 38766 - Posted: 30 Oct 2014 | 10:12:14 UTC

I'm so happy to have contributed to this research! Not only because of its undisputed significance (related to cancer and other diseases, ground-braking discovery and research, further proof for the usefulness of research done with distributed computing power), but also because of the beautiful green badge decorating my account!! :)

My faith in this project has lifted, a lot!

Congratulations!
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Message 38767 - Posted: 30 Oct 2014 | 12:51:45 UTC
Last modified: 30 Oct 2014 | 13:05:55 UTC

I would just like to add that nate writes very lucidly, which is not always the case in scientific areas. And I have never paid any attention to the badges before, but now I know that ETA and skgiven (among others) are not just collecting Christmas decorations; very impressive.

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Message 38769 - Posted: 30 Oct 2014 | 16:06:57 UTC

Congratulation! Thanks for taking the time to explain things in a manner that we laypersons can at least have a chance of wrapping our minds around your discoveries. ;-)

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Message 38774 - Posted: 31 Oct 2014 | 18:07:10 UTC

Oh grats!. One time i dont look into the forum for a week and such an important update arrives ^^
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Message 38775 - Posted: 31 Oct 2014 | 18:21:03 UTC - in response to Message 38774.

Nice, nice.

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Message 38776 - Posted: 31 Oct 2014 | 22:36:23 UTC

Cool story, bro :P
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Message 38975 - Posted: 20 Nov 2014 | 17:31:19 UTC - in response to Message 38742.

While I'm sure this is extremely exciting, I was instantly thrown back to the 80s where every Saturday morning and weekday afternoon I was inundated with commercials proclaiming KID's love KIX cereal.

I swear, I'm not dumb. Really.

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Message 38976 - Posted: 20 Nov 2014 | 17:41:19 UTC - in response to Message 38766.

I'm so happy to have contributed to this research! Not only because of its undisputed significance (related to cancer and other diseases, ground-braking discovery and research, further proof for the usefulness of research done with distributed computing power), but also because of the beautiful green badge decorating my account!! :)

My faith in this project has lifted, a lot!

Congratulations!


How do I display a cool sig like yours? I signed up in 2k6 too, the WCG site widget doesn't seem nearly as informational unlike yours.

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Message 38978 - Posted: 20 Nov 2014 | 21:35:27 UTC - in response to Message 38976.

That signature is made by this guy at WCG
https://secure.worldcommunitygrid.org/forums/wcg/viewthread?thread=29840

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Message boards : News : New publication: Our study of a disordered protein and its significance