A Comprehensive Biophysical Description of Pairwise Epistasis throughout an Entire Protein Domain


To answer this question, we quantified the effects of all single mutations and double mutations between all positions in the IgG-binding domain of protein G (GB1). By observing the first two steps of all possible evolutionary pathways using this fitness profile, we were able to characterize the extent and magnitude of pairwise epistasis throughout an entire protein molecule. Furthermore, we developed a novel approach to quantitatively determine the effects of single mutations on structural stability (DDGU). This enabled determination of the importance of stability effects in functional epistasis

Submission Details

ID: 45J9HKuN

Submitter: Connie Wang

Submission Date: July 31, 2017, 11:46 a.m.

Version: 1

Publication Details
Olson CA;Wu NC;Sun R,Curr Biol (2014) A comprehensive biophysical description of pairwise epistasis throughout an entire protein domain. PMID:25455030
Additional Information

Study Summary

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)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Protein GB 1 P06654 SPG1_STRSG
100.0 Protein GB 1 P19909 SPG2_STRSG