Article
Guidelines for protein design: the energetics of beta sheet side chain interactions.
Science (New York, N.Y.) - 10 Nov 1995
Smith C K, Regan L
Abstract excerpt
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...
Topics
- Bacterial Proteins
- Hot Temperature
- Hydrogen Bonding
- Mutation
- Protein Conformation
- Protein Denaturation
- Protein Engineering
- Protein Folding
- Protein Structure, Secondary
- Streptococcus
- Thermodynamics