Am I the only one who sees a huge disconnect between protein designs and how efficiently they can be executed in the wet-lab? What do you think it’s missing?What could be done for it be improved? Are the datasets used to train those models not good enough anymore?What do you think? Best, Omar. © ProteinReach|2026 SciLearningWorkshops LLC Unsubscribe · Preferences

I came across a nanodisc-based purification approach that just changed how I think about membrane protein biochemistry. I wish I had known about this during my PhD.This approach, developed by Cube Biotech, allows the purification of membrane binding proteins without detergents. It relies instead on a copolymer based nanodisc technology.What makes this especially compelling is that the nanodiscs create an environment that closely resembles a native cell membrane.Here is what stood out to...

Do you struggle with assessing the movement of specific residues of your protein during MDS? Here, I have a tool that can help you with that……It’s called eRMSF, and it allows you to assess the movement of residues during molecular dynamics simulation (MDS) runs at specific time points. So no need to rely on average values in a traditional RMSF plot, instead, you can complement that with eRMSF. You’ll be able to have a better sense of the types of domains, regions in your protein that are...