Arrangement of chromatin in intact chicken erythrocyte nuclei was investigated by small angle neutron scattering. The scattering spectra have revealed that on the scales between 15 nm and 1.5 lm the interior of the nucleus exhibited properties of a mass fractal. The fractal dimension of the protein component of cell nucleus held constant at approximately 2.5, while the DNA organization was biphasic, with the fractal dimension slightly higher than 2 on the scales smaller than 300 nm and approaching 3 on the larger scales.

Identification and quantitative analysis of different proteoforms (protein species) presented in a cell line generated from high grade glioblastoma was performed using two-dimensional electrophoresis (2DE), mass spectrometry (ESI LC-MS/MS), and immunodetection. A 2DE protein map containing an extensive data set comprising 937 spots with 1542 unique protein identifications (proteoforms) of 600 genes was obtained. Additionally, another set of experiments was performed where 16012 proteoforms coded by 4050 genes were identified by MS/MS according to their position in 96 gel sections (pixels). A special attention has been paid to the proteins that are the potential biomarkers of glioblastoma. The list of these biomarkers was compiled from literature. Next, we generated the graphs with theoretical and experimental information about proteoforms coded by the same gene. Such a virtualexperimental representation allowed better visualization of the state of these gene products. Many proteins, potential biomarkers of glioblastoma as well, are characterized by high numbers of protein species. We assume that these species could be a potential source of highly specific biomarkers of glioblastoma.

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