Journal article

CIRCULAR DICHROIC INVESTIGATIONS OF SECONDARY STRUCTURE IN SYNTHETIC PEPTIDE INHIBITORS OF CAMP-DEPENDENT PROTEIN-KINASE - A MODEL FOR INHIBITORY POTENTIAL

J REED, V KINZEL, HC CHENG, DA WALSH

BIOCHEMISTRY | AMER CHEMICAL SOC | Published : 1987

Abstract

The structure of the inhibitory domain of the inhibitor protein of the cAMP-dependent protein kinase has been assessed by circular dichroism studies of synthetic inhibitory peptides. Using the inhibitory peptide PKI(5-22)amide (Thr5-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn- Ala-Ile22) [Cheng, H.-C., Kemp, B. E., Pearson, R. B., Smith, A. J., Misconi, L., Van Patten, S. M., & Walsh, D. A. (1986) J. Biol. Chem. 261, 989-992] and shorter peptides of this sequence, it has been estimated that this parent peptide is composed of approximately 30% alpha-helix with the remainder being random coil with one beta-turn. The pseudosubstrate arginine cluster (Arg15-Arg19) is within the s..

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