Chemical Communications

Two prolines with a difference: contrasting stereoelectronic effects of 4 R/S-aminoproline on triplex stability in collagen peptides [Pro (X)-Pro (Y)-Gly] n

M Umashankara, IR Babu, KN Ganesh

文献索引：Umashankara; Babu, I Ramesh; Ganesh, Krishna N Chemical communications (Cambridge, England), 2003 , # 20 p. 2606 - 2607

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被引用次数: 17

摘要

Collagen is the most abundant structural protein in mammals and its mechanical properties are related to the high thermal stability of its triple helical structure. 1 The primary structure of collagen is characterized by a repeating X–Y–Gly triplet motif. Proline is the most abundant residue in the triple helix, with the Y-position mostly occupied by trans-4R-hydroxyproline. While this amino acid causes remarkable collagen stabilization when present in the Y position, ...