The website is a great idea. Thanks for suggesting it. It might be a while - I'm overwhelmed with research at the moment! If you'd like to help design a page, I wouldn't say no!

It is both a research project and a fund-raising effort to support the research project. There is no money to be made here - we do everything on very tight research budgets and everything we discover goes into the public domain. The crowdrise fund-raising effort had two goals: (1) $100,000 to buy a critical piece of lab equipment - done. That instrument, an FPLC, removed a major bottle neck in our wetlab pipeline. We direct a global collaboration to find antibody therapies for Ebola virus and had such a tremendous response that we were not able to keep up with the number of samples flooding into the lab. Now that we have the instrument, that problem is solved. (2) The second goal was to fund-raise $75,000 for the salary and health benefits of the scientist we have hired to frame projects for and analyze data from the WCG. We are about $5,000 into that project. You can see some of the questions he would like to ask about Ebola's transformer proteins in a post above.

Thank-you Dr. Saphire for all of that information. It really helps to just get a glimpse of what your team is doing and the challenges ahead. When your team is ready, we'll be ready to do what we do best...crunch the numbers for you. All the best in your preparations and the necessary funding.

Thank you very much Dr. Saphire for letting us know. The informations and the "behind the scenes" are very much appreciated.

Good question about the intrinsically disordered protein - but it's not. It's always ordered as far as we know - just ordered in different forms. A butterfly-shaped dimer (two-part structure) seems to be critical for trafficking about the cell, a ring-shaped octamer (8 parts) binds RNA and controls replication, and a linear hexamer (6 parts) forms the filamentous shell that builds and buds new copies of the virus. This is a nice write-up on it written for an educated layperson:
http://phys.org/news/2014-05-protein-insights-ebola-virus-disease.html

The important thing about it not being an intrinsically disordered protein is that the existence of multiple structures for it could not have been predicted bioinformatically - just by looking at the sequence. We came upon them quite by accident and then over five years and an awful lot of biological experiments proved that each structure was linked to a different function and that all the structures were identical. The thing about this that I think is revolutionary for biology is that this can not be the only protein that does this. I think other viruses will do it as well - it's an excellent strategy to get a lot of function out of very little genome - more bang for your buck. It makes sense that viruses would do this since they are under evolutionary pressure to maintain a compact genome. However, we could find this in human proteins as well. What if there were a protein involved in cancer that transformed its structures? The possibility that a protein exists in multiple parallel, but distinct 3D structure is not part of our common intellectual framework. We have no high-throughput assay by which we might find out if a cancer were determined by a protein being in the wrong structure. Our high throughput assays look for a mutation (no mutation here, the same wild-type sequence makes them all), or they look for gene on or off or protein present or absent (here the protein is always present - its' just formed differently). The only way we currently have to determine this is the long and expensive labor of love that is experimental structural biology. This is why I want to get a handle on the theoretical and computational parameters by which we can understand this phenomenon and learn if there are rules by which we could find this elsewhere bioinformatically.