Solvent-induced distortions and the curvature of α-helices

@article{Blundell1983SolventinducedDA,
  title={Solvent-induced distortions and the curvature of $\alpha$-helices},
  author={Tom L. Blundell and David J. Barlow and Nivedita Borkakoti and Jesse Thornton},
  journal={Nature},
  year={1983},
  volume={306},
  pages={281-283}
}
The α-helix defined in 1951 by Pauling et al. 1 on the basis of model building and X-ray fibre diffraction data has 3.65 residues per turn (n) achieved with planar peptides, torsion angles of φ = −48° and ψ = −57° and hydrogen bonds which are close to linear. Although X-ray analyses of proteins have confirmed the general correctness of the model for the helix, recent high resolution (1.7–1.0 Å) diffraction studies have shown that the parameters described by Pauling et al. 1 and later by Perutz2… Expand
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