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• W2043499342 abstract "An approach is described for the de novo design of protein-like structures in which synthetic combinatorial libraries (SCLs) were incorporated into an amphipathic α-helical scaffold (an 18-mer sequence made up of leucine and lysine residues) to generate conformationally defined SCLs. In particular, the SCLs in which the “combinatorialized” positions were on the hydrophilic face showed an α-helical conformation in mild buffer. These SCLs were used to generate context-independent but position-dependent scales of α-helical propensity for the L-amino acids. These scales were then used to design highly α-helical peptides that self-associated in mild buffer. The same approach was also found to permit the identification of conformation-dependent decarboxylation catalysts. An approach is described for the de novo design of protein-like structures in which synthetic combinatorial libraries (SCLs) were incorporated into an amphipathic α-helical scaffold (an 18-mer sequence made up of leucine and lysine residues) to generate conformationally defined SCLs. In particular, the SCLs in which the “combinatorialized” positions were on the hydrophilic face showed an α-helical conformation in mild buffer. These SCLs were used to generate context-independent but position-dependent scales of α-helical propensity for the L-amino acids. These scales were then used to design highly α-helical peptides that self-associated in mild buffer. The same approach was also found to permit the identification of conformation-dependent decarboxylation catalysts." @default.
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• W2043499342 date "1996-02-01" @default.
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• W2043499342 title "Functionalized Protein-like Structures from Conformationally Defined Synthetic Combinatorial Libraries" @default.
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• W2043499342 doi "https://doi.org/10.1074/jbc.271.8.4120" @default.
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