A 27-mer tandem repeat polypeptide in bovine amelogenin: synthesis and CD spectra.
CD spectra of a tandem 27-mer repeat polypeptide, Gln-Pro-His-Gln-Pro-Leu-Gln-Pro-His-Gln-Pro-Leu-Gln-Pro-Met-(Gln-Pro-Leu)4, from bovine amelogenin synthesized by standard solid-phase synthesis manifests an archtypical CD pattern of a beta-spiral structure in phosphate buffer at pH 5.2 and trifluoroethanol (TFE), CF3OH. beta-spiral structure is unique to a class of diverse proteins including amelogenins conferring unusual physicochemical properties.
Renugopalakrishnan
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Harvard Medical School, Children's Hospital, Boston, MA 02115, USA. Renu@biofold.net
D053523:Amelogenin; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003746:Dental Enamel Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D017433:Protein Structure, Secondary; D020449:Repetitive Sequences, Amino Acid; D014270:Trifluoroethanol
D053523:Amelogenin; D003746:Dental Enamel Proteins; D010455:Peptides; D014270:Trifluoroethanol