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: May 15, 2017, 1:19 p.m.

Version: 2

Publication Details
Smith CK;Regan L,Science (1995) Guidelines for protein design: the energetics of β sheet side chain interactions PMID:7481801
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
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)

Correlation with other assays (exact sequence matches)