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  • Title: Nonprolyl cis peptide bonds in unfolded proteins cause complex folding kinetics.
    Author: Pappenberger G, Aygün H, Engels JW, Reimer U, Fischer G, Kiefhaber T.
    Journal: Nat Struct Biol; 2001 May; 8(5):452-8. PubMed ID: 11323723.
    Abstract:
    Folding of tendamistat, an inhibitor of alpha-amylase, is a fast two-state process accompanied by two minor slow reactions, which were assigned to prolyl isomerization. In a proline-free variant, 5% of the molecules still fold slowly with a rate constant of 2.5 s(-1). This reaction is caused by a slow equilibrium between two populations of unfolded molecules. The time constant for this equilibration process, its sensitivity to LiCl and its temperature dependence identify it as a cis-trans isomerization of nonprolyl peptide bonds. Although nonprolyl peptide bonds have the cis conformation populating only approximately 0.15% in unfolded proteins, their large number generates a significant fraction of slow-folding molecules. This emphasizes that heterogeneous populations in an unfolded protein can induce complex folding kinetics on various time scales.
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