Influence of proline hydroxylation upon the thermal stability of collagen fragment α1CB2

Conformational study of a collagen peptide by 1H NMR spectroscopy: observation of the 14N‐1H spin‐spin coupling of the Arg guanidinium moiety in the triple‐helix structure

“…It contains 36 residues, 33% being imino acids. Circular dichroism and NMR spectra showed that CB2 molecules fold into a triple helical conformation at low temperature as other collagen peptides do and in agreement with previous reports on CB2 [9–11]. Arg 9 is in position Y and represents a suitable probe to experimentally verify the hypothesis set forth by Yang et al [4]concerning the possible stabilising effect of the Arg residue on the collagen structure.…”

Conformational analysis and stability of collagen peptides by CD and by1H- and13C-NMR spectroscopies

“…In the case of CB2 only there is an equilibrium between homoserine and its lactone, and there is probably also incomplete hydroxylation of some of the six prolyl residues in the Y position. As demonstrated by Ward and Mason, 41 the stability of CB2 from rat tail tendon and skin is influenced by the different extent of prolyl hydroxylation (P/Hyp ϭ 2.75 and 1.4 mol/mol in the two tissues, respectively). The original report on the bovine CB2 sequence 42 does not mention prolyl underhydroxylation for any of the six prolyl residues in the Y position but reports an excess of Pro over Hyp following amino acid analysis (P/Hyp ϭ 6.5/5.6 mol/ mol).…”

Calculation of the Structures of Collagen Models. Role of Interchain Interactions in Determining the Triple-Helical Coiled-Coil Conformation. 2. Poly(glycyl-prolyl-hydroxyprolyl)

“…23 Similarly, there is an 8 K difference in Tm of the 36-residue proteolytic fragments alCB2 obtained from rat skin collagen and rat-tail tendon collagen. 24 The degree of hydroxylation and Tm are higher in the 0024-9297/80/2213-0470$01.00/0 © 1980 American Chemical Society The end groups used in the computation are shown.…”