Conformational preferences of substituted prolines in the collagen triple helix.
Conformational preferences of substituted prolines in the collagen triple helix.
复制标题
胶原三螺旋中取代脯氨酸的构象偏好。
DOI：
10.1002/bip.10123
复制
发表时间：
2002
期刊：
影响因子：
2.9
通讯作者：
Klein,TeriE
中科院分区：
文献类型：
--
作者：
Mooney,SeanD;Kollman,PeterA;Klein,TeriE
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–Amp1+–Gly)10]3, and [(Pro–Flp–Gly)10]3in 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
