Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids.

@article{Dames2006ResidualDC,
  title={Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids.},
  author={Sonja A Dames and Regula Aregger and Navratna Vajpai and Pau Bernad{\'o} and Martin Blackledge and Stephan Grzesiek},
  journal={Journal of the American Chemical Society},
  year={2006},
  volume={128 41},
  pages={13508-14}
}
Residual dipolar couplings (RDCs) observed by NMR in solution under weak alignment conditions can monitor average net orientations and order parameters of individual bonds. By their simple geometrical dependence, RDCs bear particular promise for the quantitative characterization of conformations in partially folded or unfolded proteins. We have systematically investigated the influence of amino acid substitutions X on the conformation of unfolded model peptides EGAAXAASS as monitored by their… CONTINUE READING

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