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Accelerating the Interplay Between Theory and Experiment in Protein Design

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Figure 2-1:  The core residues of Gβ1 designed in this study.   Each of these positions was allowed to assume various rotamers of the hydrophobic amino acids Ala, Val, Ile, Leu, Phe, Tyr, and Trp
Figure 2-2: General scheme used to design combinatorial mutation libraries based on computational protein design calculations
Table 2-1: Combinatorial libraries designed from different sources of structural information
Table 2-2: Library coverage.  For each design problem, we report the number of top 20 and top 100 designed sequences from each original list that were represented in each corresponding combinatorial library
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