Guidelines for Protein Design: The Energetics of β Sheet Side Chain Interactions
- 10 November 1995
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 270 (5238) , 980-982
- https://doi.org/10.1126/science.270.5238.980
Abstract
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.Keywords
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