Influence of hydrophobic interactions on the conformational adaptability of the beta-Ala residue.

@article{Thakur2001InfluenceOH,
  title={Influence of hydrophobic interactions on the conformational adaptability of the beta-Ala residue.},
  author={A. K. Thakur and Raghuvansh Kishore},
  journal={The journal of peptide research : official journal of the American Peptide Society},
  year={2001},
  volume={57 6},
  pages={455-61}
}
The chemical synthesis and X-ray crystal structure analysis of a model peptide incorporating a conformationally flexible beta-Ala residue: Boc-beta-Ala-Pda, 1 (C23H46N2O3: molecular weight = 398.62) have been described. The peptide crystallized in the crystal system triclinic with space group P21: a = 5.116(3) A, b = 5.6770(10) A, c = 21.744(5) A; alpha = 87.45 degrees, beta = 86.87 degrees, gamma = 90.0 degrees; Z = 1. An attractive feature of the crystal molecular structure of 1 is the… CONTINUE READING

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