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• W2748562364 abstract "This thesis is based on the studies that have been carried out in the Department of Structural Research at the Max Planck Institute for Biochemistry from December 2000 to January 2004. Two projects were undertaken. The first was the study of function and interactions of cell cycle proteins and cell differentiation proteins. The proteins studied were retinoblastoma protein (pRb), cyclin-dependent kinase 6 (CDK6) and cell differentiation factors MyoD and Id-2. The second project focused on structural and dynamic investigations on photoactive proteins green fluorescent protein (GFP), cyan fluorescent protein (CFP) and alpha subunit of phycoerythrocyanin (α-PEC). Cell growth and differentiation require precise interplay between cell cycle and differentiation factors. Because much of the data about the interactions between proteins crucial for this interplay is contradictory, the aim of the study was to find whether pivotal cell cycle proteins (pRb, and CDK6) can interact directly with myogenic differentiation promoting (MyoD) and inhibiting (Id–2) factors. These potential interactions were tested with pull down assays, gel filtration, mass spectroscopy, and the nuclear magnetic resonance (NMR) spectroscopy. We found that there are no direct protein–protein interactions in vitro. Indirect modulation of gene expression level of these proteins is therefore proposed. In addition we have also shown that the C–terminal part of human and chicken MyoD does not interact with human cycline-dependent kinase 6, contrary to the recent report about such a interaction taking place. The NMR characterization of the GFP and CFP created an opportunity for investigation of their dynamic properties. Newly adopted method of in vitro protein production allowed us to make 15N–His labeled samples of GFP without any cross–labeling to other amino acids. This probe allowed for identification of peaks corresponding to the important residues that interact with the chromophore (e.g. His148). The 15N - HSQC NMR spectra of the H148G GFP mutant and selectively labeled histidine samples indicated the presence of two conformations of the protein in slow exchange on the NMR time scale. Also the 19F NMR studies of variants of GFP and CFP labeled with fluorinated tryptophans, supported by temperature-, concentration- and folding-dependent experiments, provided direct evidence for the existence of a slow exchange process between two different conformational states of CFP. Photoisomerization of holoprotein α–PEC involves E – Z isomerization around a double bond in the chromophore. In our research we could observe how the two states of the chromophore influence the structure of protein. Using 15N – HSQC we observed double peaks that indicate existence of both E and Z conformations in α–PEC in the 566 nm form (made by 500 nm light irradiation). Moreover our experimental data suggest that the E form (induced by 577 nm irradiation) is conformationally unstable. Both the E and Z forms have some degree of inhomogenety with respect to the conformation of the protein. We found additionally that the E form undergoes dynamic changes in protein conformation due to interconversion to the Z form, even in darkness. This process does not affect UV/VIS spectroscopic properties of form E but it certainly affects the structure of the protein." @default.
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• W2748562364 date "2004-01-01" @default.
• W2748562364 modified "2023-09-23" @default.
• W2748562364 title "Structural and Functional Studies on Photoactive Proteins and Proteins Involved in Cell Differentiation" @default.
• W2748562364 hasPublicationYear "2004" @default.
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