A systematic structural comparison of all solved small proteins (4-6 kDa) reveals the weight of disulfide bonds in proteins' foldability
M. H. Moreira, F. C. L. Almeida, T. Domitrovic, F. L. Palhano
The paper compares the structural features of small proteins with and without disulfide bonds, finding that bonded proteins have more apolar residues exposed to solvent and are harder to predict with Robetta.
bioRxiv · Mar 30, 2021 · PreprintBiochemistry