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
Index: Umashankara; Babu, I Ramesh; Ganesh, Krishna N Chemical communications (Cambridge, England), 2003 , # 20 p. 2606 - 2607
Full Text: HTML
Citation Number: 17
Abstract
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, ...
Related Articles:
[Mayer; Ramanjulu; Vera; Pfizenmayer; Joullie Journal of Organic Chemistry, 1994 , vol. 59, # 18 p. 5192 - 5205]
Synthesis and Evaluation of Prolyl Carbamate Nucleic Acids (PrCNA)
[Meena; Kumar; Ganesh Nucleosides, Nucleotides and Nucleic Acids, 2001 , vol. 20, # 4-7 p. 1193 - 1196]