Guidelines for protein design: the energetics of β-sheet side chain interactions
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.
Submission Details
ID: NnfEHu5G
Submitter: Admin Admin
Submission Date: July 31, 2017, 11:46 a.m.
Version: 2
Publication Details
Smith CK;Regan L,Science (1995) Guidelines for protein design: the energetics of β sheet side chain interactions PMID:7481801Additional Information
Study Summary
| Number of data points | 73 |
| Proteins | Protein Gβ1 |
| Unique complexes | 33 |
| Assays/Quantities/Protocols | Experimental Assay: ΔΔG (346K) mutant pairs ; Experimental Assay: ΔΔG (346K) single mutants ; Experimental Assay: Δ(ΔΔG) ; Experimental Assay: Tm |
| Libraries | ΔΔG and Tms of pairwise mutants at positions 44 and 53 (Table 2) ; ΔΔG of single mutants at positions 44 and 53 (ref 14) ; Free energy of pairing for pairwise mutants at positions 44 and 53 (cross-strand pairs on antiparallel β-sheet) (Table 1) |
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
|---|
Data Distribution
Studies with similar sequences (approximate matches)