Context-dependent contributions of backbone hydrogen bonding to β-sheet folding energetics

@article{Deechongkit2004ContextdependentCO,
  title={Context-dependent contributions of backbone hydrogen bonding to β-sheet folding energetics},
  author={S. Deechongkit and H. Nguyen and E. Powers and P. Dawson and M. Gruebele and J. W. Kelly},
  journal={Nature},
  year={2004},
  volume={430},
  pages={101-105}
}
  • S. Deechongkit, H. Nguyen, +3 authors J. W. Kelly
  • Published 2004
  • Chemistry, Medicine
  • Nature
    • Backbone hydrogen bonds (H-bonds) are prominent features of protein structures; however, their role in protein folding remains controversial because they cannot be selectively perturbed by traditional methods of protein mutagenesis. Here we have assessed the contribution of backbone H-bonds to the folding kinetics and thermodynamics of the PIN WW domain, a small β-sheet protein, by individually replacing its backbone amides with esters. Amide-to-ester mutations site-specifically perturb… CONTINUE READING
    View on Springer
    ncbi.nlm.nih.gov
    231 Citations
    Highly Influential Citations
    8
    Background Citations
    42
    Methods Citations
    12
    Results Citations
    4
    231 Citations
    Citation Type

    Citation Type

    The Role of Backbone Hydrogen Bonds in the Transition State for Protein Folding of a PDZ Domain
    • 8
    • PDF
    Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold.
    • 30
    • PDF
    Understanding the mechanism of beta-sheet folding from a chemical and biological perspective.
    • 46
    Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states.
    • 6
    Probing the role of backbone hydrogen bonds in protein-peptide interactions by amide-to-ester mutations.
    • 35
    Backbone-Backbone H-Bonds Make Context-Dependent Contributions to Protein Folding Kinetics and Thermodynamics: Lessons from Amide-to-Ester Mutations.
    • 51
    Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.
    • 58
    Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in β-sheet folding.
    • 51
    Probing Backbone Hydrogen Bonds in Proteins by Amide‐to‐Ester Mutations
    • 5
    β-Sheet folding mechanisms from perturbation energetics
    • 35

    References

    SHOWING 1-10 OF 30 REFERENCES
    Probing backbone hydrogen bonds in the hydrophobic core of GCN4.
    • 38
    An experimental approach to evaluating the role of backbone interactions in proteins using unnatural amino acid mutagenesis.
    • 92
    Using flexible loop mimetics to extend Φ-value analysis to secondary structure interactions
    • 74
    • PDF
    Design, Synthesis, and Characterization of 4-Ester CI2, a Model for Backbone Hydrogen Bonding in Protein α-Helices
    • 45
    Hydrogen bonding stabilizes globular proteins.
    • 226
    The folding mechanism of a -sheet: the WW domain1
    • 257
    Comparative analysis of two different amide-to-ester bond mutations in the beta-sheet of 4-oxalocrotonate tautomerase.
    • 15
    Ultrafast folding of WW domains without structured aromatic clusters in the denatured state
    • 86
    • PDF
    Stereochemical Requirements for β-Hairpin Formation: Model Studies with Four-Residue Peptides and Depsipeptides
    • 171
    Dominant forces in protein folding.
    • K. Dill
    • Chemistry, Medicine
    • Biochemistry
    • 1990
    • 3,103
    • PDF