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I'm sure there are a number of presigious biology awards. You might want to look at this page http://folding.stanford.edu/English/Awards Here's one example:Adam A. Wanderer wrote:Yes, but there's nothing like a Nobel Prize to move your standing up in the scientific community. It just sort of "says something".
But, there are other awards. The "Fields" award for mathematics is only awarded every four years and is considered an even higher award in the Mathematics community. I wonder if Biology has a "super" award. Does anyone know of a really hard to get Biology award?
June 2006: Folding@home Principle Investigator Vijay Pande wins the Irving Sigal Young Investigator Award from the Protein Society. From their web site: "The Irving Sigal Young Investigator Award, sponsored by Merck Research Laboratories, recognizes a significant contribution to the study of proteins by a scientist who is in the early stages of an independent career and, generally, not more than 40 years of age at the time of the award. The 2006 awardee is Dr. Vijay Pande (Stanford University) for his unique approach to employing advances in algorithms that make optimal use of distributed computing, which places his efforts at the cutting edge of simulations. The results have stimulated a re-examination of the meaning of both ensemble and single-molecule measurements, making Dr. Pande's efforts pioneering contributions to simulation methodology."
I agree; if possible, it would be nice to know what general disease type corresponds to the project we are folding. A little personal satisfaction that we made a difference in this or that specific arena. The current descriptions are a little over my head.The FAH projects related to the above research are between 7700 and 7712. We greatly appreciate the help from all the FAH donors, beta testers, and the rest of the FAH team to make our research on molecular recognition possible.
VijayPande wrote:In terms of big picture highlights, we spent the first 5-6 years working out how to use distributed computing to efficiently tackle protein folding and then applying it to do the first simulations of protein folding reaching the folded state with experimental validation, etc. This was one of our primary goals laid out in the Science section and we're excited to have accomplished that. Part of our work today involves continuing in that direction with more complex systems, continuing to push the state of the art.
The other part of our work is to apply these methods to study disease, especially Alzheimer's Disease (AD) and Huntington's Disease (HD). We are interested in understanding what's going on in these diseases to facilitate a cure. Indeed, our motto in big letters on our web page is "Our goal: to understand protein folding, misfolding, and related diseases," and we are on track for that. One could ask "how do you know if you understand the disease?" A good answer is new small molecule drugs which appear to prevent or minimize the effects of the disease. This too is in the works, with encouraging results in the lab (but it's not time to talk about this publicly until it passes peer review).
However, it takes a long time (often as much as 2-3 years) from the point where we have something interesting in the lab to where we are talking about the results publicly (it has to be validated by ourselves and go through peer review). Our first results on AD and HD will hopefully be coming out soon, i.e. in the next 6 to 12 months or so.
Finally as for a cure -- a cure takes a while to test and develop. First, one has to understand what's going on and that's where basic science comes in and most of what FAH does. However, we and others are excited to take the published results from FAH and apply them to real world problems such as AD and HD and our expectation is that our work could give some critical insights into these diseases, thereby helping to accelerate a cure.
http://fah-web.stanford.edu/cgi-bin/fah ... ned?p=8051Huntington's disease is caused due to the presence of poly-glutamine repeats, which associate together to form toxic clumps in neuronal brain cells, leading to cell death and the associated overall neurodegenerative consequences. These repeats of glutamine are attached to one end of the Huntingtin protein. Interestingly, previous publications have shown that a small fragment at the end of the Huntingtin protein, known as N17, accelerates the creation of the toxic clumps. Although there have been several proposed mechanisms of its role, N17's exact role in this process remains largely unknown. In this project, we perform simulations of several fragments of the Huntington protein in an attempt to discover the role of this fragment and its implications in Huntington's disease. For more detailed and technical description of the project, you can read a publication by former pande group member Nicholas W. Kelley (Kelley et. al., Journal of Molecular Biology, 2009).