Guidelines for Protein Design: The Energetics of β Sheet Side Chain Interactions

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Science  10 Nov 1995:
Vol. 270, Issue 5238, pp. 980-982
DOI: 10.1126/science.270.5238.980


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.