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How Structural and Physicochemical Determinants Shape Sequence Constraints in a Functional Enzyme
2015
PLoS ONE
The need for interfacing structural biology and biophysics to molecular evolution is being increasingly recognized. One part of the big problem is to understand how physics and chemistry shape the sequence space available to functional proteins, while satisfying the needs of biology. Here we present a quantitative, structure-based analysis of a high-resolution map describing the tolerance to all substitutions in all positions of a functional enzyme, namely a TEM lactamase previously studied
doi:10.1371/journal.pone.0118684
pmid:25706742
pmcid:PMC4338278
fatcat:hcf7wjllirhl3jxggjq3jndnru