0000000001131375

AUTHOR

Jane M. Vanderkooi

showing 2 related works from this author

Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Horseradish peroxidase

1991

For the first time, conformational relaxation processes have been measured in a small protein, mesoporphyrin-horseradish peroxidase via their influence on spectral diffusion broadening of holes burnt in the fluorescence excitation spectrum of free base mesoporphyrin. Holes were burnt in three 0----0 bands of different tautomeric forms of the chromophore at 1.5 and 4 K, and the spectral diffusion broadening was measured in temperature cycling experiments between 4 and 30 K. The inhomogeneous linewidth for the tautomeric 0----0 bands was estimated to be 60-70 cm-1; the hole width was found narrow, being in the order of 350 MHz (10(-2) cm-1) at 1.5 K what allowed for an extremely sensitive det…

PhotochemistryProtein ConformationChemistryDiffusionRelaxation (NMR)Fluorescence spectrometryBiophysicsTemperature cyclingChromophorePhotochemistryTautomerLaser linewidthSpectrometry FluorescenceThermodynamicsHorseradish PeroxidaseExcitationResearch ArticleBiophysical Journal
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Photochemical holes under pressure: Compressibility and volume fluctuations of a protein

1991

From the pressure induced frequency shift of photochemical holes burnt into mesomorphyrin substituted horseradish peroxidase, we determined the compressibility of the protein and the vacuum frequency of the chromophore. From the compressibility, an estimation of the volume fluctuations of the biomolecule is possible.

chemistry.chemical_classificationAbsorption spectroscopybiologyChemistryBiomoleculeGeneral Physics and AstronomyA proteinFrequency shiftChromophorePhotochemistryHorseradish peroxidaseVolume (thermodynamics)biology.proteinCompressibilityPhysical and Theoretical ChemistryThe Journal of Chemical Physics
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