Engineering a beta-sheet protein toward the folding speed limit.

Houbi Nguyen, Marcus Jäger, Jeffery W Kelly, Martin Gruebele

Journal: The journal of physical chemistry. B 2007;109(32):15182-6

PMID: 16852923

Full Text on American Chemical Society View on PubMed

Abstract

Recent experimental studies have shown that alpha-helical proteins can approach the folding "speed limit", where folding switches from an activated to a downhill process in free energy. beta-sheet proteins are generally thought to fold more slowly than helix bundles. However, based on studies of hairpins, folding should still be able to approach the microsecond time scale. Here we demonstrate how the hPin1 WW domain, a triple-stranded beta-sheet protein with a sharp thermodynamic melting transition, can be engineered toward the folding "speed limit" without a significant loss in thermal denaturation cooperativity.

DOI: 10.1021/jp052373y

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MeSH Terms: Amino Acid Sequence, Humans, Kinetics, Models, Molecular, Molecular Sequence Data, NIMA-Interacting Peptidylprolyl Isomerase, Nonlinear Dynamics, Peptidylprolyl Isomerase, Protein Denaturation, Protein Engineering, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Temperature