07-28-2005, 10:12 PM
Found this on the F@H site, explains some of the science:
How proteins self-assemble into their native state (responsible for biological function) has been a much studied problem for over a decade. Progress has been made into how simple models of proteins fold as well as means to design protein sequences de novo. However, these models ignore much protein detail which is likely crucial for understanding how real proteins fold. Thus, the current challenge lies in understanding how particular chemical detail in proteins (such as hydrogen bonding and hydrophic interactions) lead to particular protein folding mechanisms.
We have developed techniques which allows us to make fundamental advances in simulations of protein folding, by speeding atomistic simulations 100 to 1,000 times. This speedup allows us to simulate tens of microseconds and thus simulate the folding of the fastest folding proteins in all-atom detail. However, these methods are extremely computationally demanding, and require 1000's to 10,000's of computers. To solve this problem, we have released our software as a screen saver and have gathered over 10,000 collaborators who run our software. This project, called Folding@home has already lead to great initial results (the folding of proteins in atomistic detail on the microseconds timescale) and we are now continuing to use this technique on other systems as well, including the folding of RNA and non-biological polymers as well as the aggregation of proteins associated with diseases, such as Altzheimer's and Mad Cow (see below).
How proteins self-assemble into their native state (responsible for biological function) has been a much studied problem for over a decade. Progress has been made into how simple models of proteins fold as well as means to design protein sequences de novo. However, these models ignore much protein detail which is likely crucial for understanding how real proteins fold. Thus, the current challenge lies in understanding how particular chemical detail in proteins (such as hydrogen bonding and hydrophic interactions) lead to particular protein folding mechanisms.
We have developed techniques which allows us to make fundamental advances in simulations of protein folding, by speeding atomistic simulations 100 to 1,000 times. This speedup allows us to simulate tens of microseconds and thus simulate the folding of the fastest folding proteins in all-atom detail. However, these methods are extremely computationally demanding, and require 1000's to 10,000's of computers. To solve this problem, we have released our software as a screen saver and have gathered over 10,000 collaborators who run our software. This project, called Folding@home has already lead to great initial results (the folding of proteins in atomistic detail on the microseconds timescale) and we are now continuing to use this technique on other systems as well, including the folding of RNA and non-biological polymers as well as the aggregation of proteins associated with diseases, such as Altzheimer's and Mad Cow (see below).
Daily driver 1: 2007 Jeep Wrangler Unlimited Sport "S"
33" BFG Mud-Terrain KM2s, lots of Rough Country gear - bumper, 2.5" lift, swaybar disconnects, Superwinch 10,000lb winch, Detroit Locker in rear D44 axle, custom exhaust, K+N filtercharger, Superchips-tuned.
Daily driver 2: 2006 Subaru Legacy GT
COBB Stage 1+ package - AccessPort tuner, COBB intake and airbox. Stage 2 coming shortly - COBB 3" AT stainless DP and race cat, custom 3" Magnaflow-based exhaust and Stage 2 COBB tune.
33" BFG Mud-Terrain KM2s, lots of Rough Country gear - bumper, 2.5" lift, swaybar disconnects, Superwinch 10,000lb winch, Detroit Locker in rear D44 axle, custom exhaust, K+N filtercharger, Superchips-tuned.
Daily driver 2: 2006 Subaru Legacy GT
COBB Stage 1+ package - AccessPort tuner, COBB intake and airbox. Stage 2 coming shortly - COBB 3" AT stainless DP and race cat, custom 3" Magnaflow-based exhaust and Stage 2 COBB tune.