GLOBULAR PROTEIN SPATIAL STRUCTURE STUDY BY TRITIUM PLANIGRAPHY - SHORT PEPTIDES AS A MODEL OF FULLY EXTENDED POLYPEPTIDE-CHAINстатья

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Дата последнего поиска статьи во внешних источниках: 29 мая 2015 г.

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[1] GEDROVICH A., BADUN G. Globular protein spatial structure study by tritium planigraphy - short peptides as a model of fully extended polypeptide-chain // Molecular Biology. — 1992. — Vol. 26, no. 3. — P. 427–431. The interaction of tritium atoms with amino acid residues from short peptides was studied. Such peptides may serve as a model of a fully extended polypeptide chain. Every residue in this chain had 100% steric accessibility. There was a linear correlation between the residue accessible surface area (made up of hydrocarbon fragments) and the amount of tritium reacting with this residue. The presence of the tertiary carbon atom in the residue side chain significantly affects the reactivity of the residue. There is no significant effect on the interaction of this residue with tritium atoms when this residue is at the N- and C-ends of the peptide. The reactivity scale of of the amino acid residues is compared with experimental and theoretical data in the literature.

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