[Study of the spatial structure of globular proteins by tritium planigraphy. Short peptides as a model of a fully extended polypeptide chain].
The interaction of tritium atoms with amino acid residue from short peptides was studied. The short peptides were considered as a model of extended polypeptides chain. Every residue in this chain has 100% steric accessibility. It was shown that: 1. The linear correlation exists between the residue accessible surface area (that is composed of hydrocarbon fragments) and the amount of tritium interacting with this residue; 2. The presence of the tertiary carbon atom in the residue side chain influences on the reactivity of this residue; 3. The N- or C-terminal residue presence does not influences on the possibility of interaction of this residue with tritium atoms. The obtained reactivity scale of amino acid residues is compared with other theoretical and experimental data.
Gedrovich
A V
AV
Badun
G A
GA
D000596:Amino Acids / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D014316:Tritium / Q000737:chemistry
D000596:Amino Acids; D010455:Peptides; D011506:Proteins; D014316:Tritium
Issledovanie prostranstvennoĭ struktury globuliarnykh belkov metodom tritievoĭ plantigrafii. Korotkie peptidy kak model' polnost'iu razvernutoĭ polipeptidnoĭ tsepi.