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Proceedings Paper

FT-IR Spectroscopy: The Detection Of Pressure-Induced Changes In The Secondary Structure Of Proteins
Author(s): Patrick T. T. Wong; Henry H. Mantsch
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Paper Abstract

The study of pressure-induced protein:protein interactions, and in particular the pressure-induced denaturation and dissociation of oligomeric proteins, has gained considerable interest in recent years. It is now well recognized that the protein transformation known under the general name of denaturation is a physical process which affects the three dimensional protein structure,leading to chain unfolding and/or refolding. Denaturation can be induced by changes in temperature or pressure, and by the addition of denaturing agents. The rationale for using pressure to study protein denaturation is that pressure variations at constant temperature only affect the volume of the protein, unlike the more commonly used temperature denaturation, which affects both the volume and the kinetic properties of the protein.

Paper Details

Date Published: 8 May 1989
PDF: 8 pages
Proc. SPIE 1057, Biomolecular Spectroscopy, (8 May 1989); doi: 10.1117/12.951647
Show Author Affiliations
Patrick T. T. Wong, National Research Council of Canada (Canada)
Henry H. Mantsch, National Research Council of Canada (Canada)


Published in SPIE Proceedings Vol. 1057:
Biomolecular Spectroscopy
Robert R. Birge; Henry H. Mantsch, Editor(s)

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