Another one: http://boinc.fzk.de/poem/
Our project
The figure illustrates the predicted (red) and the experimental (green) structure of the bacillus suptilus major cold shock protein, an universal nucleic acid binding domain. Such proteins are important for gene regulation under environmental stress.
Proteins are the nanoscale machinery of all the known cellular life. Amazingly, these large biomolecules with up to 100,000 atoms fold into unique three-dimensional shapes in which they function. These functions include all cellular chemistry (metabolism), energy conversion (photosynthesis) and transport (oxygen transport), signal processing in the brain (neurons), immune response and many others, often with an efficiency unmatched by any man-made process. Protein malfunction is often related to diseases and thousands disease-related proteins have been identified to date, many with still unknown structure. To understand, control or even design proteins we need to study protein structure, which is experimentally much harder to obtain than the information about the chemical composition (sequence) of a specific protein.
By joining this project you will contribute to a computational approach to
*
predict the biologically active structure of proteins
*
understand the signal-processing mechanisms when the proteins interact with one another
*
understand diseases related to protein malfunction or aggregation
*
develop new drugs on the basis of the three-dimensions structure of biologically important proteins.
POEM@HOME implements a novel approach to understand these aspects of protein structure, which lends itself very well to worldwide distributed computing. The scientific approach behind POEM@HOME is a computational realization of the thermodynamic hypothesis that won C. B. Anfinsen the Nobel Prize in Chemistry in 1972.
So please help us, by joining POEM@HOME, solve the scientific mysteries described above and decipher the biological information encoded in proteins of unknown structure.
Our project
The figure illustrates the predicted (red) and the experimental (green) structure of the bacillus suptilus major cold shock protein, an universal nucleic acid binding domain. Such proteins are important for gene regulation under environmental stress.
Proteins are the nanoscale machinery of all the known cellular life. Amazingly, these large biomolecules with up to 100,000 atoms fold into unique three-dimensional shapes in which they function. These functions include all cellular chemistry (metabolism), energy conversion (photosynthesis) and transport (oxygen transport), signal processing in the brain (neurons), immune response and many others, often with an efficiency unmatched by any man-made process. Protein malfunction is often related to diseases and thousands disease-related proteins have been identified to date, many with still unknown structure. To understand, control or even design proteins we need to study protein structure, which is experimentally much harder to obtain than the information about the chemical composition (sequence) of a specific protein.
By joining this project you will contribute to a computational approach to
*
predict the biologically active structure of proteins
*
understand the signal-processing mechanisms when the proteins interact with one another
*
understand diseases related to protein malfunction or aggregation
*
develop new drugs on the basis of the three-dimensions structure of biologically important proteins.
POEM@HOME implements a novel approach to understand these aspects of protein structure, which lends itself very well to worldwide distributed computing. The scientific approach behind POEM@HOME is a computational realization of the thermodynamic hypothesis that won C. B. Anfinsen the Nobel Prize in Chemistry in 1972.
So please help us, by joining POEM@HOME, solve the scientific mysteries described above and decipher the biological information encoded in proteins of unknown structure.