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GUIDELINES FOR PROTEIN DESIGN - THE ENERGETICS OF BETA-SHEET SIDE-CHAIN INTERACTIONS
Author(s): SMITH CK, REGAN L
Source: SCIENCE    Volume: 270    Issue: 5238    Pages: 980-982    Published: NOV 10 1995  
Times Cited: 187     References: 23     
Abstract: 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.
Document Type: Article
Language: English
Addresses:
1. YALE UNIV, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06520 USA
Publisher: AMER ASSOC ADVAN SCIENCE, 1333 H ST NW, WASHINGTON, DC 20005
Subject Category: Multidisciplinary Sciences
IDS Number: TD878
ISSN: 0036-8075
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