The conformation of human growth hormone (hGH) as monomer and aggregate as well as of those immobilized in the soluble polysaccharide matrix was investigated. The immobilization resulted in ten per cent decrease of the amount of alpha-helix and in the conformational mobility change of aromatic amino acid side groups. It did not, however, influence the biological activity of the hormone, thus suggesting that the above conformational variations did not affect functionally important portions of the molecule.
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