molecular
order (Payne & Veis, 1988).
The second derivatives of the amide I band (Fig. 3b) were calculated
to enhance resolution of the spectral bands and to minimise
baseline variations. The WP group exhibited a high proportion of
intermolecular cross-linking with decreased aggregated helices
and similar b-turn conformations compared to the FP group,
deduced from the intensity in the absorbance range of 1675–
1699 cm1 (Doyle et al., 1975). Alternatively, second derivatives
of the amide I band of FP spectra indicates a prevalence of triple
helix (1660 cm1), suggesting a more aggregated collagen structure
compared with the WP group and also a lesser amount of single
helix (1655 cm1), which is also consistent with the greater
amount of Pro, Hyp and Hyl in the FP samples and the denaturation
enthalpy (Table 2).