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Figure 2
(a) Experimental setup of in situ SAXS measurements and the 2D SAXS pattern from sample N-CR (corresponding 1D plots shown in Fig. S3), showing changes during the uncoiling of the collagen triple helix and the disordering of its intermolecular structure in the fibrils when temperature increases. (b)–(e) Radially integrated 1D SAXS profiles of reduced collagen samples to highlight peak intensity changes. (f)–(m) Changes in D-period obtained from in situ SAXS data analysis during heat denaturation of the collagen in bovine skins [N = non-reduced, R = reduced, CT = control (pH = 8), DH = dehaired (pH = 8), AC = acidified (pH = 3), CR = crosslinked (pH = 4)]. The onset temperatures (Tonset) of the D-period during denaturation are calculated and labelled alongside each curve.

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 27| Part 5| September 2020| Pages 1376-1381
https://doi.org/10.1107/S1600577520009479
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