2000
DOI: 10.1021/jp992454s
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Study of the Dynamic Structure of Native and Hydrophobized Glucose Oxidase by Time-Domain Dielectric Spectroscopy

Abstract: The dynamic structures of native and hydrophobized (by covalent attachment of palmitoyl chains) glucose oxidase were studied by time-domain dielectric spectroscopy (TDDS). Analysis of the dipole correlation function for both types of the enzyme showed that the decay of the correlation function of the macromolecule motion can be presented as a sum of components corresponding to different kinds of protein motion: isotropic rotation of the protein molecule as a whole, anisotropic Brownian tumbling of subunits, an… Show more

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Cited by 3 publications
(1 citation statement)
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“…First, characterizing the relaxation processes that appeared from the complex dielectric permittivity, curve-fitting procedures were carried out. It should be mentioned here that multiple relaxation processes were extracted from the complex dielectric spectrum by different groups [30][31][32] for different systems. We have applied the same method to extract the possible relaxation processes for the present system.…”
Section: Resultsmentioning
confidence: 99%
“…First, characterizing the relaxation processes that appeared from the complex dielectric permittivity, curve-fitting procedures were carried out. It should be mentioned here that multiple relaxation processes were extracted from the complex dielectric spectrum by different groups [30][31][32] for different systems. We have applied the same method to extract the possible relaxation processes for the present system.…”
Section: Resultsmentioning
confidence: 99%