Designing a 20-residue protein

Truncation and mutation of a poorly folded 39-residue peptide has produced 20-residue constructs that are >95% folded in water at physiological pH. These constructs optimize a novel fold, designated as the 'Trp-cage' motif, and are significantly more stable than any other miniprotein re...

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Published inNature structural & molecular biology Vol. 9; no. 6; pp. 425 - 430
Main Authors Andersen, Niels H, Neidigh, Jonathan W, Fesinmeyer, R. Matthew
Format Journal Article
LanguageEnglish
Published United States Nature Publishing Group 01.06.2002
Subjects
Circular Dichroism
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Models, Molecular
Mutation
Peptides
Peptides - chemistry
Peptides - metabolism
Protein Conformation
Protein Denaturation
Protein Engineering
Protein Folding
Proteins - chemistry
Proteins - metabolism
Thermodynamics
Tryptophan - chemistry
Tryptophan - metabolism
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Summary:Truncation and mutation of a poorly folded 39-residue peptide has produced 20-residue constructs that are >95% folded in water at physiological pH. These constructs optimize a novel fold, designated as the 'Trp-cage' motif, and are significantly more stable than any other miniprotein reported to date. Folding is cooperative and hydrophobically driven by the encapsulation of a Trp side chain in a sheath of Pro rings. As the smallest protein-like construct, Trp-cage miniproteins should provide a testing ground for both experimental studies and computational simulations of protein folding and unfolding pathways. Pro-Trp interactions may be a particularly effective strategy for the a priori design of self-folding peptides.
Bibliography:ObjectType-Article-1
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ISSN:1072-8368
1545-9993
2331-365X
1545-9985
DOI:10.1038/nsb798