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iancook221188
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Default 07-09-2015, 13:59 | posts: 1,716 | Location: uk

From the Official FAH Blog:
http://folding.stanford.edu/home/blog


Quote:
First full version of our Folding@Home client for Android Mobile phones
July 7, 2015 by Vijay Pande ·

We’re proud to announce the first full version of our Folding@Home client for Android Mobile phones. This version is available to all Android Mobile phones with version 4.4 (Kitkat) and above. Thanks to suggestions by donors we have redesigned the user interface and added new features such as:

contribute processing time continuously: just connect to a WiFi network and a charger.
one can login to Google Game Services, earn collaboration achievements, compete against his / her friends in processing time.
collaborate processing time from multiple devices under the same Google Game Services account.
settings screen has been removed. No need to configure anything!
details about the currently selected research type can be queried by touching the Research Type title on main screen, or by choosing “Active Research” on menu.

Scientifically, as in our previous beta run, we continue to focus on breast cancer with our mobile app. In this project, we’re investigating the nature of drug resistance mutations in key proteins (kinases) that are targets for breast cancer drugs. By studying the nature of how these mutations change these key drug targets, we will be able to both advance our basic biophysical understanding of these key proteins as well as build a tool to be used for patient specific breast cancer treatment— by sequencing the tumor and seeing what mutations are present, our tool seeks to recommend the best drug for a specific patient.

The beta has been a success with positive feedback from our community. We plan to add additional features in the comming months to further enhance the user interface and experience. The beta version has been downloaded more than 170,000 times worldwide, with more than 62,000 mobile phones contributing at the same time. We want to thank our community for your feedback and continued support.

We’ve also added a new movie to advertise and highlight the app. It’s on YouTube here:

https://www.youtube.com/watch?v=Ayjw-NTMXdo
   
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iancook221188
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Default 07-18-2015, 10:49 | posts: 1,716 | Location: uk

From the Official FAH Blog:
http://folding.stanford.edu/home/blog

Quote:
Simulating protein dynamics to find binding-competent states
July 15, 2015 by Vincent Voelz ·

Mutation to the tumor-suppressor protein p53 is a common feature in most cancers. MDM2–a protein whose job it is to downregulate p53 via their direct binding interaction–has therefore become a prime target for cancer therapeutics. Normally, a small helical region of p53 binds the MDM2 receptor site, but if a molecule with a similar shape can bind the receptor site of MDM2 strongly enough, it can prevent p53 from binding, thus making more p53 available to perform its tumor suppression abilities.

Many different kinds of molecular mimics of the p53 helix have been designed to disrupt the p53-MDM2 interaction, including stapled peptides, cyclic hairpin peptides, beta-peptides, peptoids (N-substituted oligoglycines), oligoarylamides, and spiroligomers, just to name a few. These molecules are much larger than typical small-molecule drugs, and have interesting folding properties that must be overcome to achieve tight binding. Stapled peptides, for instance, feature a hydrocarbon “staple” that helps rigidify the helical conformation in solution, which in turn enhances the binding affinity.

Using molecular simulations on Folding@home, we have been studying the coupled folding and binding of the p53 helix to MDM2 to address several key questions. One goal is to understand the roles the conformational dynamics in shaping the binding mechanism – such information can ultimately help to design better-binding molecular mimics.

Another question is whether or not molecular dynamics simulations can be used to discover binding-competent receptor conformations of MDM2 in the absence of a bound crystal structure. In new work from our lab (Pantelopulos et al. Proteins 2015), we show that ligand-free simulations of MDM2 starting from conformations with a closed binding cleft can sample open-cleft conformations capable of binding. We also tested the performance of several recent force field models in predicting experimental NMR measurements. We found that that all of the force fields perform similarly well, but that longer simulations (out to a microsecond) result in better agreement with experiment.

You can read about our work in the latest issue of Proteins:

Microsecond simulations of MDM2 and its complex with p53 yield insight into force field accuracy and conformational dynamics George A. Pantelopulos and Vincent A. Voelz. Proteins: Structure, Function and Bioinformatics, Accepted (2015)
   
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iancook221188
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Videocard: GTX 670 SLI / GTX 460 SLI
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PSU: TX850 / AX850
Default 08-09-2015, 21:29 | posts: 1,716 | Location: uk

From the Official FAH Blog:
http://folding.stanford.edu/home/blog

Quote:
A global view of FAH Mobile Client usage
August 5, 2015 by Mark Piercy ·

People around the world are continuing to help advance research by downloading and running Folding@home mobile.

Here is an image of the global usage distribution of our Mobile Client created by Pande group member Muneeb Sultan. This shows all current connections from mobile phones to our Workserver here at Stanford University during a given time period.
   
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