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Conformational preferences of substituted prolines in the collagen triple helix
Author(s) -
Mooney Sean D.,
Kollman Peter A.,
Klein Teri E.
Publication year - 2002
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.10123
Subject(s) - chemistry , triple helix , collagen helix , stereochemistry , crystallography
Researchers have recently questioned the role hydroxylated prolines play in stabilizing the collagen triple helix. To address these issues, we have developed new molecular mechanics parameters for the simulation of peptides containing 4(R)‐fluoroproline (Flp), 4(R)‐hydroxyproline (Hyp), and 4(R)‐aminoproline (Amp). Simulations of peptides based on these parameters can be used to determine the components that stabilize hydroxyproline over proline in the triple helix. The dihedrals F–C–C–N, O–C–C–N, and N–C–C–N were built using a N‐β‐ethyl amide model. One nanosecond simulations were performed on the trimers [(Pro–Pro–Gly) 10 ] 3 , [(Pro–Hyp–Gly) 10 ] 3 , [(Pro–Amp–Gly) 10 ] 3 , [(Pro–Amp 1+ –Gly) 10 ] 3 , and [(Pro–Flp–Gly) 10 ] 3 in explicit solvent. The results of our simulations suggest that pyrrolidine ring conformation is mediated by the strength of the gauche effect and classical electrostatic interactions. © 2002 Wiley Periodicals, Inc. Biopolymers 64: 63–71, 2002