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Register4Less,

I thought I'd write and let you know that being nice, ethical, and giving money to a cartoonist does, oddly enough, work.

Until last week, I had my domain names, [xxxxxxxxxx].com and [xxxxx].net, registered through Go Daddy simply because they were cheap and I didn't have any particular problems with them.

That changed when they decided it would be a good idea to try to phone me under the guise of conducting some sort of customer satisfaction survey and try to get me to spend more money on products I don't need (waking my mother up in the process!).

After being told I was not available at the moment, they decided to send a condescending email asking me to update my "invalid" phone number (it was not invalid, it was just intentionally not the easiest way to get hold of me; any emergencies would have resulted in my being contacted within minutes).

Being the sole full-time sysadmin for an understaffed Silicon Valley startup trying to run an enterprise-grade service, not possessing a driver's licence, and living 700+ miles from any friends or family that could aid me in my already overloaded days, and on top of it trying to keep my own personal servers up and running, I barely have time to do my own laundry. I don't have time to deal with telemarketing, and I was extremely disappointed that an internet company, who should understand better than anyone how valuable it is to be able to triage and prioritize communications via email, would try to interrupt my day with phone calls of no importance whatsoever.

I was just going to reply with a nasty note. Then I realized it was time I started speaking a language corporations would understand. I decided to transfer my domains, and having read UF for years, R4L was the obvious choice. Your sponsorship of UserFriendly and Illiad's enthusiasm about it gave you instant credibility. Your privacy policy and free whois privacy completed the trifecta. Go Daddy got a nasty note, you got a happily-spent $30, and I got one less thing to worry about.

You've got a customer for life.

Many thanks to Nicholas for the very nice letter. There's more room at the UF.R4L inn. Bring your domains! :)

FIRST WCG PAPER PUBLISHED: The first Human Proteome Folding project paper, titled Superfamily Assignments for the Yeast Proteome through Integration of Structure Prediction with the Gene Ontology has been published.

This (the very first) World Community Grid enabled paper is based on yeast, which was used as a control in the HPF experiments since it is so well understood. As an indication of the timescales involved in academic research, the paper was first submitted in May 2006, and was only published this month (March 2007).

There are a number of other papers also pending publication, so more papers should emerge from the pipeline in a steady trickle. This should give those people with a serious interest in the science something to chew over!

As promised, the results have been published in public, and the paper has a Creative Commons Public Domain declaration. Thank you all for helping make the paper possible. Here's a snippet:

Author Summary:

"The three-dimensional structure of a protein can reveal much about that protein's evolutionary relationships and functions. Such information about all the proteins in an organism-the proteome-would offer a more global view of these relationships, but solving each structure individually would be a formidable task. In this study, we have parsed all Saccharomyces cerevisiae proteins into nearly 15,000 distinct domains and then used de novo structure prediction methods together with worldwide distributed computing to predict structures for all domains lacking sequence similarity to proteins of known structure. To overcome the uncertainties in de novo structure prediction, we combined these predictions with data on the biological process, function, and localization of the proteins from previous experimental studies to assign the domains to families of evolutionarily related proteins. Our genome-wide domain predictions and superfamily assignments provide the basis for the generation of experimentally testable hypotheses about the mechanism of action for a large number of yeast proteins."

And I hardly need add: if you haven't already, please join Team UserFriendly.Org