Paper
8 May 1989 FT-IR Spectroscopy: The Detection Of Pressure-Induced Changes In The Secondary Structure Of Proteins
Patrick T. T. Wong, Henry H. Mantsch
Author Affiliations +
Proceedings Volume 1057, Biomolecular Spectroscopy; (1989) https://doi.org/10.1117/12.951647
Event: OE/LASE '89, 1989, Los Angeles, CA, United States
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.
© (1989) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Patrick T. T. Wong and Henry H. Mantsch "FT-IR Spectroscopy: The Detection Of Pressure-Induced Changes In The Secondary Structure Of Proteins", Proc. SPIE 1057, Biomolecular Spectroscopy, (8 May 1989); https://doi.org/10.1117/12.951647
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Cited by 4 scholarly publications.
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KEYWORDS
Proteins

Infrared radiation

Spectroscopy

Raman spectroscopy

FT-IR spectroscopy

Diamond

Fourier transforms

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