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Alternative Computational Protocols for Supercharging Protein Surfaces for Reversible Unfolding and Retention of Stability

Figure 7

Specific examples of hydrogen bonds removed by AvNAPSA supercharge.

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.

Figure 7