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Science 10 November 1995:
Vol. 270. no. 5238, pp. 980 - 982
DOI: 10.1126/science.270.5238.980
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Reports

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

Catherine K. Smith and Lynne Regan (1)

To determine the interaction energy between cross-strand pairs of side chains on an antiparallel beta 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 beta sheet propensities. The experimental results paralleled the statistical frequency with which the residue pairs are found in beta sheets of known structure.


Department of Molecular Biophysics and Biochemistry,
Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.
(1) To whom correspondence should be addressed.


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