Protein aggregation studied by forward light scattering and light transmission analysis

Penzkofer, Alfons and Shirdel, J. and Zirak, P. and Breitkreuz, H. and Wolf, E. (2007) Protein aggregation studied by forward light scattering and light transmission analysis. CHEMICAL PHYSICS, 342 (1-3). pp. 55-63. ISSN 0301-0104, 1873-4421

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Abstract

The aggregation of the circadian blue-light photo-receptor cryptochrome from Drosophila melanogaster (dCry) is studied by transmission and forward light scattering measurement in the protein transparent wavelength region. The light scattering in forward direction is caused by Rayleigh scattering which is proportional to the degree of aggregation. The light transmission through the samples in the transparent region is reduced by Mic light scattering in all directions. It depends on the degree of aggregation and the monomer volume fill factor of the aggregates (less total scattering with decreasing monomer volume fill factor of protein globule) allowing a distinction between tightly packed protein aggregation (monomer volume fill factor 1) and loosely packed protein aggregation (monomer volume fill factor less than 1). An increase in aggregation with temperature, concentration, and blue-light exposure is observed. At a temperature of 4 degrees C and a protein concentration of less than 0.135 mM no dCry aggregation was observed, while at 24 degrees C and 0.327 mM gelation occurred (loosely packed aggregates occupying the whole solution volume). (C) 2007 Elsevier B.V. All rights reserved.

Item Type: Article
Uncontrolled Keywords: SPECTROSCOPIC CHARACTERIZATION; INDOCYANINE GREEN; DROSOPHILA; PHOTORECEPTOR; SIZE; Rayleigh scattering; Mie scattering; static light scattering; light scattering; protein aggregation; Drosophila cryptochrome
Subjects: 500 Science > 530 Physics
Divisions: Physics > Institute of Experimental and Applied Physics > Alumni or Retired Professors > Group Alfons Penzkofer
Depositing User: Dr. Gernot Deinzer
Date Deposited: 25 Nov 2020 07:36
Last Modified: 25 Nov 2020 07:36
URI: https://pred.uni-regensburg.de/id/eprint/31810

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