Modulating Collagen Triple-Helix Stability with 4-Chloro, 4-Fluoro, and 4-Methylprolines
Collagen is a fibrous protein comprising a right-handed, triple-helical bundle of three parallel, left-handed polyproline II-type helices. Each strand consists of approximately 300 repeats of the trimer (Xaa-Yaa-Gly), where Xaa is often (2S)-proline (Pro) and Yaa is often (2S,4R)-4-hydroxyproline (Hyp) . The most abundant protein in vertebrates, collagen is of fundamental importance to the three-dimensional architecture of such animals. Understanding the chemical determinants of the structure and stability of collagen is essential for both curing collagen-related diseases and creating collagen-based biomaterials.
KeywordsTriple Helix Collagenous Peptide Synthetic Collagen Collagen Triple Helix Stereoelectronic Effect
This work was supported by grant AR44276 (NIH). M.D.S. was supported by a graduate fellowship from the Department of Homeland Security.
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