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Quantum‐mechanical study of model molecules in relation to collagen structure. II. (Gly‐Phe‐Pro) and (Gly‐Pro‐Phe) repeating units
Author(s) -
Cabrol Daniel,
Broch Henri,
Vasilescu Dane
Publication year - 1981
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1981.360200203
Subject(s) - tripeptide , chemistry , molecule , residue (chemistry) , pyrrolidine , stereochemistry , triple helix , collagen helix , ring (chemistry) , peptide , quantum chemical , crystallography , biochemistry , organic chemistry
Abstract A conformational quantum‐mechanical study of (Gly‐Phe‐Pro) and (Gly‐Pro‐Phe) repeating tripeptide sequences has been carried out with the PCILO method. Using appropriate molecules as a model, we investigated the conformational possibilities of each in situ residue. Computations have been done taking into account the two typical pyrrolidine ring puckering and the most favorable orientations of the phenylalanyl side chain. Major conclusions drawn from this study are that the phenylalanyl can be accommodated at both second and third positions in the sequence without preventing the formation of triple‐helix conformation. However, the analogy observed between the rotational possibilities around the second residue of Gly‐Pro‐Pro and Gly‐Phe‐Pro indicates that phenylalanyl in the second position favors the triple‐helix formation.