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: Oct. 24, 2016, 12:14 p.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
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