As FIDA relies on changes in hydrodynamics radius, it works best for small targets such as motifs from IDPs.

Luckily, this is what we intended to use it for 😉

Crucial to the screening is the lab scale protein expression pipeline below.

We use an old trick beloved by the IDR-community for protein purication: Heat lysis.

Due the thermostability of the binders, we get ~95% pure lysate after a heating step in 96-well plates.

dx.doi.org/10.17504/pro...

The technique works best for small targets with a large change in radius of hydration upon binding – e.g. SLiMs in IDPs 😊 – but also works for larger proteins with only a 10% change in RH upon binding.

We find that it works excellently with “boiling lysis” – exploiting the high thermostability of binder designs to remove endogenous proteins – and then simply dilution the supernatant with buffer before measurement.

FIDA measure radius of hydration based on diffusion in a microfluidic capillary.

This allows us to pick out successful binders based on the increase in R_H – a one-point measurement for initial screening and titration for affinity determination.

The bulk of the prize comes in the form of a grant for educational development.

We plan to use this to integrate computational skills - mainly python and R - across the whole curriculum. The prize allows us to hire someone the spearhead this across all the courses in our department!

This is part of a new series of teaching prizes spanning from primary school to university level by the Novo Nordisk Foundation.

Seen from the outside, it looks like a 💰-push to increase the public and institutional recognition of teaching. Interesting to see how this will evlve.