Conformational studies of the human complex-forming glycoprotein, heterogeneous in charge: protein HC

Human complex-forming glycoprotein, heterogeneous in charge, is a single polypeptide chain widely distributed in physiological fluids. The conformation of the protein has been studied with attention to the secondary and tertiary structures. Circular dichroism and predictive methods from the amino acid sequence have been employed for the characterization of the secondary structure. This is composed of 20% alpha-helix, 21% beta-structure, 29% beta-turns, 30% aperiodic conformation, and an average number of residues per helical segment of nine. Titration of the protein indicated the existence of two groups for the tyrosine residues, each of them composed of three and five residues. The four tryptophan residues of the molecule are located in two different polarity microenvironments, according to the fluorescence studies. These observations are corroborated by studying the hydropathic profile of the protein. From this study, three different domains are observed in the protein, one of them being exposed and containing the main part of the unordered structure of the molecule. The chromophore naturally associated with the protein has been resolved in three fluorescent units not dependent on the protein conformation. These bands have been observed centered around 290, 360, and 410 nm, which do not correspond to any described chromophore.