To determine the interaction energy between cross-strand pairs of side chains on an antiparallel β sheet, pairwise amino acid substitutions were made on the solvent-exposed face of the B1 domain of streptococcal protein G. The measured interaction energies were substantial (1.8 kilocalories per mole) and comparable to the magnitude of the β sheet propensities. The experimental results paralleled the statistical frequency with which the residue pairs are found in β sheets of known structure.
Submitter: Admin Admin
Submission Date: May 15, 2017, 1:19 p.m.
|Number of data points||73|
|Assays/Quantities/Protocols||Experimental Assay: ΔΔG (346K) mutant pairs ; Experimental Assay: ΔΔG (346K) single mutants ; Experimental Assay: Δ(ΔΔG) ; Experimental Assay: Tm|
|Libraries||Free energy of pairing for pairwise mutants at positions 44 and 53 (cross-strand pairs on antiparallel β-sheet) (Table 1) ; ΔΔG of single mutants at positions 44 and 53 (ref 14) ; ΔΔG and Tms of pairwise mutants at positions 44 and 53 (Table 2)|