[Typical tripeptide sequences of collagen: quantitative conformation study].
Theoretical and experimental investigations on the conformations of synthetic polytripeptides, with Gly-R2-R3 general repetitive sequence, are of great interest for the comprehension of the factors which contribute to the triple helix stabilization. Using appropriate molecules as models, we have investigated by the PCILO method the intrinsic conformational possibilities of each "in situ" residue for the following cases : Gly-imino-imino, Gly-amino-imino and Gly-imino-amino which represent the most important sequences occurring in the primary structure of collagen. The computations were carried out taking into account the two pyrrolidine ring puckerings and the preferential side-chains orientations. Extending our previous work concerning the isomeric polytripripeptides Gly-X-Pro and Gly-Pro-X with X epsilon (Pro, Phe) we have studied the cases of X epsilon (Ala, Ser). In this brief communication, we present a preliminary synthesis of these recent results.
D000595:Amino Acid Sequence; D003094:Collagen; D007536:Isomerism; D011487:Protein Conformation; D013816:Thermodynamics
D003094:Collagen
Séquences tripeptidiques typiques du collagène: étude conformationnelle quantique.