Helix formation in reduced, S-carboxymethylated human choriogonadotropin beta subunit and tryptic peptides.

Journal of Protein Chemistry
D Puett, S Birken

Abstract

The beta subunit of human choriogonadotropin (hCG beta) and its asialoderivative were digested with trypsin and then reduced and S-carboxymethylated. A series of peptides were purified which corresponded to residues 1-43, 44-95, 96-114, and 123-145 of the 145 amino acid residue glycoprotein. The two N-linked oligosaccharides were present on the amino terminal peptide, and three of the four O-linked oligosaccharides were present on the carboxy terminal peptide. Circular dichroic spectra between 190-240 nm were obtained on reduced, S-carboxymethylated (RCM) hCG beta and the above peptides, both in aqueous solution and in the helicogenic solvent 80% (vol/vol) trifluoroethanol (TFE). In aqueous solution there was evidence of only limited helicity in the peptides and RCM-hCG beta; however, in the presence of TFE, peptides 1-43 and 44-95 exhibited significant helicity, as did the full-length linear chain. The helicity developed in TFE by RCM-hCG beta appears much greater than that which occurs in the native, disulfide-intact form, thus suggesting that the disulfides prevent expression of helicity in regions with alpha-helix potential. Application of the Chou-Fasman secondary structure predictive algorithm to hCG beta suggested that s...Continue Reading

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