Summary
X-ray diffraction analyses have provided detailed structural information on the 310-helices of (i) pBrBz-d-(αMe)Phe-(Aib)2-d-(αMe)Phe-Aib-OtBu and Ac-(Aib)2-l-Lys(Bz)-(Aib)2-l-Lys(Bz)-(Aib)2-NHMe as suitable templates for molecular recognition studies, and (ii) pBrBz-TOAC-(l-Ala)2-TOAC-l-Ala-NHtBu as an appropriate spacer for an ESR study of side chain to side chain interactions. In addition, in Ac-TOAC-(Aib)2-l-Trp-Aib-OMe, forming a 310-helix, the TOAC residue plays the role of an effective quencher of the fluorescence of the tryptophan residue located one turn apart.
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References
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Crisma, M., Bianco, A., Formaggio, F. et al. The polypeptide 310-helix as a template and a spacer. Lett Pept Sci 2, 187–189 (1995). https://doi.org/10.1007/BF00119149
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DOI: https://doi.org/10.1007/BF00119149