Experiments with proteins at low temperature: what do we learn on properties in their functional state?

The authors compared the spectral response of Zn-substituted horseradish peroxidase in a glycerol/water solvent to hydrostatic pressure at 2 K and ambient temperature. The low temperature experiments clearly demonstrate the presence of at least three different conformations with drastically differen...

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Veröffentlicht in:	The Journal of chemical physics 2007-04, Vol.126 (16), p.165104-165104
Hauptverfasser:	Ponkratov, V V, Wiedersich, J, Friedrich, J, Vanderkooi, J M
Format:	Artikel
Sprache:	eng
Schlagworte:	Heme - chemistry Horseradish Peroxidase - chemistry Hydrostatic Pressure Protein Structure, Tertiary Spectrometry, Fluorescence Temperature Zinc - chemistry
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description	The authors compared the spectral response of Zn-substituted horseradish peroxidase in a glycerol/water solvent to hydrostatic pressure at 2 K and ambient temperature. The low temperature experiments clearly demonstrate the presence of at least three different conformations with drastically different elastic properties. However, the main conformation, which determines the fluorescence spectrum at ambient temperature, did not show any significant difference between low and high temperature and pressure. The authors conclude that the local compressibility of the heme pocket of the protein depends only very weakly on temperature.
doi_str_mv	10.1063/1.2723731
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subjects	Heme - chemistry Horseradish Peroxidase - chemistry Hydrostatic Pressure Protein Structure, Tertiary Spectrometry, Fluorescence Temperature Zinc - chemistry
title	Experiments with proteins at low temperature: what do we learn on properties in their functional state?
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