Redesigning Protein Cavities as a Strategy for Increasing Affinity in Protein-Protein 
                        Interaction: Interferon-<b><i>γ</i></b> Receptor 1 as a Model

<div>Nonreducing 12.5% SDS-PAGE gel of selected monomeric refolded recombinant His-tagged IFN<i>γ</i>R1 variants. Proteins were extracted from inclusion bodies by 8 M urea, further purified on Ni-NTA agarose, and dialyzed, and monomeric fraction was separated on gel filtration column (see above). IFN<i>γ</i>R1 with C-terminal His-Tag migrates at a molecular mass of 23 kDa when analyzed on nonreducing SDS-PAGE gel.</div>

BioMed Research International

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Figure 1

Figure 1: Redesigning Protein Cavities as a Strategy for Increasing Affinity in Protein-Protein 
                        Interaction: Interferon-<b><i>γ</i></b> Receptor 1 as a Model 

Figure 1 | Redesigning Protein Cavities as a Strategy for Increasing Affinity in Protein-Protein 
                        Interaction: Interferon-γ Receptor 1 as a Model 

BioMed Research International

Redesigning Protein Cavities as a Strategy for Increasing Affinity in Protein-Protein Interaction: Interferon-γ Receptor 1 as a Model

Figure 1