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Investigation of pH‐Dependent Collagen Triple‐Helix Formation
Author(s) -
Lee SongGil,
Lee Jee Yeon,
Chmielewski Jean
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200802224
Subject(s) - triple helix , polyproline helix , collagen helix , hydroxyproline , chemistry , helix (gastropod) , peptide , monomer , stereochemistry , crystallography , biochemistry , biology , organic chemistry , polymer , ecology , snail
Helices on demand : Collagen peptides were engineered to form triple helices under environmental control. The replacement of the hydroxyproline (Hyp) residues in a collagen peptide with carboxylate‐modified Hyp residues gave a petide that forms a collagen triple‐helical structure at acidic pH values and low temperatures and adopts a monomeric, polyproline II helical conformation under neutral conditions (see scheme).