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Updated: Jul 19, 2026

Magnetic Tweezers for the Measurement of Twist and Torque
Published on: May 19, 2014
Metal-assisted stabilization and probing of collagenous triple helices
Takaki Koide1, Maki Yuguchi, Mayuka Kawakita
1Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima, Japan. tkoide@bio.tokushima-u.ac.jp
Abstract:
Collagen model peptides that contain 2,2'-bipyridyl (bpy) ligands were designed and synthesized. The thermal stability of the collagenous triple helix was increased by forming an Fe(II)(bpy-peptide)(3) complex. The chirality of the metal center was shifted to form right-handed Delta-isomers induced by the supercoiling of the peptide moiety. Moreover, the refolding rate of the triple helix was increased in the presence of Fe(II). This metal-coordinating system possesses potential to be used to stabilize the triple-helical conformation as well as to probe the folding status of collagen model peptides.
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