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  • Title: Assessing computational amino acid beta-turn propensities with a phage-displayed combinatorial library and directed evolution.
    Author: Hsu HJ, Chang HJ, Peng HP, Huang SS, Lin MY, Yang AS.
    Journal: Structure; 2006 Oct; 14(10):1499-510. PubMed ID: 17027499.
    Abstract:
    Structure propensities of amino acids are important determinants in guiding proteins' local and global structure formation. We constructed a phage display library--a hexa-HIS tag upstream of a CXXC (X stands for any of the 20 natural amino acids) motif appending N-terminal to the minor capsid protein pIII of M13KE filamentous phage--and developed a novel directed-evolution procedure to select for amino acid sequences forming increasingly stable beta-turns in the disulfide-bridged CXXC motif. The sequences that emerged from the directed-evolution cycles were in good agreement with type II beta-turn propensities derived from surveys of known protein structures, in particular, Pro-Gly forming a type II beta-turn. The agreement strongly supported the notion that beta-turn formation plays an active role in initiating local structure folding in proteins.
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