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- W2552945555 abstract "We aimed to explore the differences of thermal behaviors between insoluble collagen fibrils (ICFs) and pepsin-solubilized collagens (PSCs) from sea cucumber Stichopus japonicus. The unfolding/refolding sequences of secondary structures of ICFs and PSCs during the heating and cooling cycle (5 → 70 → 5 °C) were identified by Fourier transform infrared spectrometry combined with curve-fitting and 2D correlation techniques. ICFs showed a higher proportion of α-helical structures and higher thermostability than PSCs, and thus had more-stable triple helical structures. The sequences of changes affecting the secondary structures during heating were essentially the same between ICFs and PSCs. In all cases, α-helix structure was the most important conformation and it disappeared to form a β-sheet structure. In the cooling cycle, ICFs showed a partially refolding ability, and the proportion of β-sheet structure rose before the increasing proportion of α-helix structure. PSCs did not obviously refold during the cooling stage." @default.
- W2552945555 created "2016-11-30" @default.
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- W2552945555 date "2016-11-16" @default.
- W2552945555 modified "2023-10-14" @default.
- W2552945555 title "Unfolding/Refolding Study on Collagen from Sea Cucumber Based on 2D Fourier Transform Infrared Spectroscopy" @default.
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- W2552945555 doi "https://doi.org/10.3390/molecules21111546" @default.
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