Abstract
The temperature and pressure dependence on the secondary structure of α-chymotrypsin was studied by FT-IR spectroscopy. The temperature dependence of the secondary structures of α-chymotrypsin indicates that the temperature-induced unfolding of α-chymotrypsin sets in at 41°C and pD 7.0 at ambient pressure. Upon unfolding, the content of intermolecular β-sheet structures increases drastically, whereas that of intramolecular β-sheets decrease concomitantly. At room temperature (21°C), this protein denatures at ~4.9 kbar. No aggregation occurs in the pressure-denaturated state. A tentative p-T stability diagram was obtained on the basis of pressure dependent FT-IR measurements at different temperatures.
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© 2003 Springer-Verlag Berlin Heidelberg
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Sun, Z., Winter, R. (2003). Temperature- and Pressure-induced Unfolding of α-Chymotrypsin. In: Winter, R. (eds) Advances in High Pressure Bioscience and Biotechnology II. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-05613-4_21
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DOI: https://doi.org/10.1007/978-3-662-05613-4_21
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-05674-1
Online ISBN: 978-3-662-05613-4
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