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Deciphering how naturally occurring sequence features impact the phase behaviours of disordered prion-like domains
The complex link between protein sequence and phase behaviour for a family of prion-like low-complexity domains (PLCDs) has now been revealed. The results have uncovered a set of rules—which are interpreted using a stickers-and-spacers model—that govern the sequence-encoded phase behaviour of such PLCDs and enable physicochemical rationalizations that are connected to the underlying sequence composition.
- Anne Bremer
- , Mina Farag
- & Tanja Mittag
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Temperature-jump solution X-ray scattering reveals distinct motions in a dynamic enzyme
Understanding how structural dynamics contribute to protein function is a longstanding challenge in structural biology. Now, time-resolved X-ray solution scattering following an infrared laser-induced temperature jump has been used to probe functional, intramolecular motions in the dynamic enzyme cyclophilin A.
- Michael C. Thompson
- , Benjamin A. Barad
- & James S. Fraser