Chapter title |
High-Pressure Fluorescence Spectroscopy.
|
---|---|
Chapter number | 32 |
Book title |
High Pressure Bioscience
|
Published in |
Sub cellular biochemistry, January 2015
|
DOI | 10.1007/978-94-017-9918-8_32 |
Pubmed ID | |
Book ISBNs |
978-9-40-179917-1, 978-9-40-179918-8
|
Authors |
Maeno, Akihiro, Akasaka, Kazuyuki, Akihiro Maeno, Kazuyuki Akasaka |
Abstract |
The combination of fluorescence and pressure perturbation is a widely used technique to study the effect of pressure on a protein system to obtain thermodynamic, structural and kinetic information on proteins. However, we often encounter the situation where the available pressure range up to 400 MPa of most commercial high-pressure fluorescence spectrometers is insufficient for studying highly pressure-stable proteins like inhibitors and allergenic proteins. To overcome the difficulty, we have recently developed a new high-pressure fluorescence system that allows fluorescence measurements up to 700 MPa. Here we describe the basic design of the apparatus and its application to study structural and thermodynamic properties of a couple of highly stable allergenic proteins, hen lysozyme and ovomucoid, using Tryptophan and Tyrosine/Tyrosinate fluorescence, respectively. Finally, we discuss the utility and the limitation of Trp and Tyr fluorescence. We discuss pitfalls of fluorescence technique and importance of simultaneous use of other high-pressure spectroscopy, particularly high-pressure NMR spectroscopy. |
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