We have evaluated the interaction energy of a three-residue ionic network constructed on the beta-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). Study holds ProTherm entries: 12839, 12840, 12841, 12842, 12843, 12844, 12845, 12846, 12847, 12848, 12849, 12850, 12851, 12852, 12853, 12854 Extra Details: beta-sheet; protein stability; protein design; electrostatics; side chain,interactions
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:44 p.m.
|Number of data points||47|
|Proteins||Immunoglobulin G-binding protein G ; Immunoglobulin G-binding protein G|
|Assays/Quantities/Protocols||Experimental Assay: ddG ; Experimental Assay: dCp temp:75.0 C ; Experimental Assay: dG ; Experimental Assay: dTm ; Experimental Assay: dCp ; Experimental Assay: Tm ; Experimental Assay: dHvH|
|Libraries||Mutations for sequence MTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE|