A Comprehensive Biophysical Description of Pairwise Epistasis throughout an Entire Protein Domain
Abstract
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:25455030Additional Information
Study Summary
| Number of data points | 1524659 |
| Proteins | Protein GB 1 |
| Unique complexes | 536942 |
| Assays/Quantities/Protocols | Experimental Assay: Selected Library ; Experimental Assay: Input Library ; Derived Quantity: Fitness |
| Libraries | All single and double mutants ; Input Library ; LN(W) |
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 |
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Data Distribution
Studies with similar sequences (approximate matches)