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Effect of hydrostatic pressure on unfolding of α-lactalbumin: Volumetric equivalence of the molten globule and unfolded state

✍ Scribed by Yoshihiro Kobashigawa; Katsutoshi Nitta; Masao Sakurai

Book ID
111753564
Publisher
Cold Spring Harbor Laboratory Press
Year
2008
Tongue
English
Weight
271 KB
Volume
8
Category
Article
ISSN
0961-8368

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Effect of hydrostatic pressure on conformational changes of canine milk lysozyme between the native, molten globule, and unfolded states
✍ Masahiro Watanabe; Tomoyasu Aizawa; Makoto Demura; Katsutoshi Nitta 📂 Article 📅 2004 🏛 Elsevier Science 🌐 English ⚖ 225 KB

The effect of pressure on the unfolding of the native (N) and molten globule (MG) state of canine milk lysozyme (CML) was examined using ultraviolet (UV) spectroscopy at pH 4.5 and 2.0, respectively. It appeared that the thermally induced unfolding was promoted by the increase of pressure from atmos