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本帖最后由 金鹏 于 2014-4-24 16:49 编辑
P9406 to full FAHby cxh » Wed Apr 23, 2014 3:15 am Here are some of the project details:
clones 5
min-core-version 46
natoms 78000
runs 1040
stats-credit 10500
timeout 3.5
deadline 4.5
In the same vein as 9401, this is a simulation of a disordered p53 peptide while binding to another protein. In this case, however, the binding partner is S100B, which is a cell cycle regulator. We hope to study how mutations in p53 may disrupt binding and, in the process, onset cancer.
Happy folding! P9408 to full FAHby cxh » Wed Apr 23, 2014 3:16 am Here are the project details:
min-core-version 46
natoms 52940
runs 6220
stats-credit 13000
timeout 10.9
deadline 14.1
This is actually a clone of project 9401. Project 9401 was retired after a work server failure. P9101 moving to advby msultan » Sat Apr 19, 2014 7:43 am Hello all,
Moving 9101 to Advanced after testing on beta. It should be pretty stable.
Project Info:
The fyn kinase is an enzyme present in multiple signaling pathways whose aberrant behavior leads to cancerous cell growth, and has also been implicated in the invasion of the dengue virus. This project continues the Pande Lab's effort to map out the conformational landscape of the src kinase family. Recent work from our lab on a similar kinase found a potentially druggable intermediate state(Shukla et al, Nature2014). The main aim of the present simulation is to get a better understanding of Fyn's dynamics in order to design better therapeutics.
More Science:
The link between fyn and dengue: http://www.ncbi.nlm.nih.gov/pubmed/23616652
Recent Src Results: http://www.nature.com/ncomms/2014/14030 ... s4397.html
Some Project Stats:
client-type beta
timeout 8.0
deadline 10.0
k-factor 0.75
gens 2000
min-core-version 46
natoms ~33000
stats-credit 4000
Cheers,
Muneeb New GPU Project 9201by jadeshi » Wed Apr 23, 2014 8:05 am Project description here: http://fah-web.stanford.edu/cgi-bin/fah ... ned?p=9201 (fah-web seems to be down at the moment of this post, however)
Transcribed (roughly):
This project is a simulation of Pin1 WW domain, which is a 40-residue protein arranged in an anti-parallel, 3-stranded beta sheet in the native state. It has been studied extensively in literature as a model system for the folding of beta sheets in general. Because beta sheets are ubiquitous structures in the proteome, gaining a firm understanding of the folding dynamics of this small representative system could potentially provide insights into the folding dynamics of countless other proteins. Experiments have suggested that the rate-limiting step to folding involves formation of the loop between the first and second strands, though no higher resolution structural information of the folding mechanism is available. This simulation will aim to establish an atomistic picture of the transition state ensemble and dominant folding pathways.
The long term vision of this project is to use the information obtained through the simulation to design small molecules to catalyze folding (i.e. stabilize the transition state). This small molecule catalysis methodology has direct applications to combating common protein misfolding diseases such as Alzheimer's and Parkinson's disease, and represents an alternative to the typical approach of directly destabilizing misfolded structures.
Specs:
OS: Win/Linux
stats credit: 4000
k-factor: 0.75
timeout: 2.6
deadline: 3.4
n_atoms: 15000
min core version: 46
contact: jadeshi@stanford.edu
Thanks!
目前转正CORE17包: 13000 13001 9406 9408
强烈建议GF110 114核心费米卡跑9201,有超常的PPD表现
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