Abstract
Charged groups play a critical role in the stability of the helix formed by the isolated C-peptide (residues 1–13 of ribonuclease A) in aqueous solution. One charged-group effect may arise from interactions between charged residues at either end of the helix and the helix dipole. We report here that studies of C-peptide analogues support the helix dipole model, and provide further evidence for the importance of electrostatic interactions not included in the Zimm–Bragg model for α-helix formation.
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Shoemaker, K., Kim, P., York, E. et al. Tests of the helix dipole model for stabilization of α-helices. Nature 326, 563–567 (1987). https://doi.org/10.1038/326563a0
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DOI: https://doi.org/10.1038/326563a0
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