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  • Title: Computer-based redesign of a protein folding pathway.
    Author: Nauli S, Kuhlman B, Baker D.
    Journal: Nat Struct Biol; 2001 Jul; 8(7):602-5. PubMed ID: 11427890.
    Abstract:
    A fundamental test of our current understanding of protein folding is to rationally redesign protein folding pathways. We use a computer-based design strategy to switch the folding pathway of protein G, which normally involves formation of the second, but not the first, beta-turn at the rate limiting step in folding. Backbone conformations and amino acid sequences that maximize the interaction density in the first beta-hairpin were identified, and two variants containing 11 amino acid replacements were found to be approximately 4 kcal mol-1 more stable than wild type protein G. Kinetic studies show that the redesigned proteins fold approximately 100 x faster than wild type protein and that the first beta-turn is formed and the second disrupted at the rate limiting step in folding.
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