Alternative Computational Protocols for Supercharging Protein Surfaces for Reversible Unfolding and Retention of Stability
In AvNAPSA designs, wild-type surface residues forming hydrogen bonds can be mutated (white sticks show the native side chain). A) Mutation of surface NQ/DE/RK residues can lead to loss of hydrogen bonds. B) Common sidechain-backbone hydrogen bonding motifs at protein surfaces mediate direct interaction with secondary structure elements and interaction with regions that transition between secondary structure elements. N and Q residues can act as both donor and acceptor, illustrating the risk of automated N to D and Q to E mutations.