Guest post: Dr. Greg Bowman, UC Berkeley
We just had a protein folding conference at Stony Brook University in New York that was extremely encouraging. Both the experimental and theoretical communities are very excited about the results we are generating with Folding@home. In particular, they are excited about (i) our increasing ability to make quantitative connections with experiments and (ii) the long timescale dynamics for large proteins we are now able to capture. For example, we recently succeeded in folding an 80-residue protein on 10 millisecond timescales (paper is here). For reference, that’s about twice as many residues and about 1,000 times longer timescales than what most anybody else is able to achieve! There are now multiple experimental groups who are asking us to make predictions for them to test. So, we appreciate all your help and have plenty of new calculations for you to contribute to.
