Investigation of pH‐Dependent Collagen Triple‐Helix Formation | Zendy

Lee SongGil | Zendy; Lee Jee Yeon | Zendy; Chmielewski Jean | Zendy

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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).

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