Dev Josh here with your weekly Foldit update.
(Disclaimer: This is not scientific feedback; these solutions are not officially endorsed by the Foldit scientists.)
Here’s what the devs have been up to lately:
Wow, that’s a ton! Bear with us while we try to roll out all of these cool new improvements. It might take us a while to get them all tested and ready to go.
Do you have trouble with getting the hydrogen bonds right on your sheets? Here’s some diagrams and explanations on the geometry of sheet bonding.
There’s a lot you can learn from your fellow players. Join a group and share your solutions! Both the sharer and the evolver tend to learn something from the process.
Until next time, happy folding!
Dev Josh here with your weekly Foldit update. Can you believe I’ve been writing these newsletters for an entire year now? The first newsletter was July 3, 2020, before binding metrics were even added to the game! What a long, strange trip it’s been.
For the veteran folders out there, LociOiling has added a bugfix to Bruno Kestemont’s Banded Worm Pairs (BWP) in versions 3.4.8 and 1.4.9.
A huge congratulations and thanks to NinjaGreg! Not only has his design of the month been synthesized in the wet lab, but he has also been volunteering with the Foldit dev team to help us fix bugs and add new features! You rock, Greg.
Given the new updates to Banded Worm Pairs (BWP), let’s break down what exactly this recipe is doing and how to use it. This is a very late game recipe for squeezing out just a couple of extra points at the very end of a puzzle. The original BWP was actually written by KarenCH and based on an even older “worm” wiggle by rav3n_pl. Since then, a number of worm recipes have spawned based on this approach. They’re crawling all over the place!
BWP uses bands and local wiggling to try to optimize your fold. The recipe usage itself is pretty simple. The slider adjusts how often you want to save progress, ranging from every time you gain 0.3 points to 1000 points from the recipe. And the textbox is for a name for the save file. These saves are stored in the Menu under Open/Share Solutions. In the later versions of this recipe, it also accounts for objectives like H-Bond Networks, and will run infinitely until you tell it to stop.
Want us to keep talking about recipes, or something else? Post your feedback on our feedback forum!
Did you know that every week, LociOiling collects even more screenshots from the top puzzle results and posts them to the Foldit Wiki? What a champ, thanks Loci! Be sure to check out those results so you can see what the top folders are doing in every puzzle!
Even though Foldit colors entire sidechains as hydrophobic or hydrophilic, this is actually a property of the individual atoms that make up a sidechain! Carbons are hydrophobic, while polar atoms like oxygen and nitrogen are hydrophilic. Keep this in mind when packing your interfaces and cores: it’s not just what sidechains you use, but how you angle them! Hydrophobicity is atomic!
We’re making some major improvements to Dojo mode! Be sure to check it out and let us know what you think on the forums or the #dojo channel of our Discord server!
Wiggle Shake Wiggle by SaveVMK and Pikamander2
This week’s art comes from Nicm25! Who knew bands could be such a great artistic tool?
Moving stuff around in Foldit can be hard. That’s why I made this guide to learn about controlling your movements in 3D space!
Do you have a recipe or screenshot to share? Send it in to email@example.com!
We’ve got some seriously exciting new things happening just around the corner! But I will let bkoep talk about it more in the next lab report. Instead, I’ll simply share some cool new scientific papers we’ve all got our eyes on:
The Baker Lab at UW has developed a protein prediction algorithm called RoseTTAFold in their latest paper Accurate prediction of protein structures and interactions using a three-track neural network. Meanwhile, literally published on the same day, DeepMind finally describes their own algorithm, AlphaFold, in their article Highly accurate protein structure prediction with AlphaFold. Could this mean we have brand new technologies for quickly identifying whether a fold will be successful? Only time will tell!
The Olympic, by Nicm25
Do you tend to cut your protein apart at the loops, but then you can’t get your loops ideal when you merge them back together? Try cutting in the middle of your sheets and helices instead! This preserves your loops better and makes it easier to idealize loops after merging.
Make sure you subscribe to our YouTube channel and click that bell icon so you get notified when our lab reports go live! You won’t want to miss this!