We have evaluated the interaction energy of a three-residue ionic network constructed on the β-sheet surface of protein G using double mutant cycles. Although the two individual ion pairs were each stabilizing by ∼0.6 kcal/mol, the excess gain in stability for the triad was small (0.06 kcal/mol).
Submitter: Marie Ary
Submission Date: March 21, 2017, 3:49 p.m.
|Number of data points||57|
|Assays/Quantities/Protocols||Experimental Assay: ΔH (Tm) ; Experimental Assay: ΔG (75°C) ; Experimental Assay: Tm pH5.5 ; Derived Quantity: ΔΔG RE(X) (75°C) ; Derived Quantity: ΔΔΔG RER (75°C)|
|Libraries||all permutations of R or I at position 6, E or A at 53, and R or A at 44 (Table 1) ; interaction energies for ion pairs and the 3-residue network|