×
Well done. You've clicked the tower. This would actually achieve something if you had logged in first. Use the key for that. The name takes you home. This is where all the applicables sit. And you can't apply any changes to my site unless you are logged in.

Our policy is best summarized as "we don't care about _you_, we care about _them_", no emails, so no forgetting your password. You have no rights. It's like you don't even exist. If you publish material, I reserve the right to remove it, or use it myself.

Don't impersonate. Don't name someone involuntarily. You can lose everything if you cross the line, and no, I won't cancel your automatic payments first, so you'll have to do it the hard way. See how serious this sounds? That's how serious you're meant to take these.

×
Register


Required. 150 characters or fewer. Letters, digits and @/./+/-/_ only.
  • Your password can’t be too similar to your other personal information.
  • Your password must contain at least 8 characters.
  • Your password can’t be a commonly used password.
  • Your password can’t be entirely numeric.
Enter the same password as before, for verification.
Login

Grow A Dic
Define A Word
Make Space
Set Task
Mark Post
Apply Votestyle
Create Votes
(From: saved spaces)
Exclude Votes
Apply Dic
Exclude Dic

Flipping Out: Role of Arginine in Hydrophobic Polymer Collapse

Click here to flash read.

arXiv:2403.11305v2 Announce Type: replace-cross
Abstract: Arginine has been a mainstay in biological formulation development for decades. To date, the way arginine modulates protein stability has been widely studied and debated. Here, we employed a hydrophobic polymer to decouple hydrophobic effects from other interactions relevant to protein folding. While existing hypotheses for the effects of arginine can generally be categorized as either direct or indirect, our results indicate that direct and indirect mechanisms of arginine co-exist and oppose each other. At low concentrations, arginine was observed to stabilize hydrophobic polymer collapse via a sidechain-dominated direct mechanism, while at high concentrations, arginine stabilized polymer collapse via a backbone-dominated indirect mechanism. These findings highlight the modular nature of the widely used additive arginine, with relevance in the design of stable biological formulations.

Click here to read this post out
ID: 809447; Unique Viewers: 0
Unique Voters: 0
Total Votes: 0
Votes:
Latest Change: March 29, 2024, 7:33 a.m. Changes:
/u/anonymous
Dictionaries:
Words:
Spaces:
Views: 13
CC:
No creative common's license
Comments: