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Dynamical Behaviour of Matrix Proteins from Mason-Pfizer Monkey Virus
Srb, Pavel ; Lang, Jan (advisor) ; Žídek, Lukáš (referee) ; Brus, Jiří (referee)
Title: Dynamical behaviour of matrix proteins from Mason-Pfizer Monkey Virus Author: Pavel Srb Department: Department of Low temperature physics Supervisor: doc. RNDr. Jan Lang, PhD. Abstract: We studied the oligomeric properties of betaretroviral nonmyristoylated ma- trix protein (MA) and its R55F mutant from the Mason-Pfizer monkey virus in solution by means of NMR spectroscopy. We have proven that the wild- type (WT) MA forms oligomers in solution. The final model of oligomeriza- tion of the WT MA was derived by concerted use of chemical shift mapping and diffusion-ordered spectroscopy measured on a set of protein samples with varying concentrations. We found that the Mason-Pfizer monkey virus WT MA exists in a monomer-dimer-trimer equilibrium in solution. Further a combination of NMR relaxation measurements and advanced analysis of molecular dynamics simulation trajectory provided an unprecedentedly de- tailed insight into internal mobility of matrix proteins of the Mason-Pfizer monkey virus. Strong evidence have been obtained that the oligomerization capacity of the wild-type matrix protein is closely related to the enhanced dynamics of several parts of its backbone on a nanosecond time scale. In- creased flexibility has been observed for two regions: the loop between he- lices α2 and α3 and the C-terminal...
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Solid-state NMR study of structure and segmental dynamics of pharmaceutical materials based on the solid dispersions of drugs in polymer matrices.
Policianová, Olívia ; Brus, Jiří (advisor) ; Smrček, Stanislav (referee) ; Dračínský, Martin (referee)
Highly-exact structural characterization is the crucial step in the development and manufacturing process of pharmaceutical materials. Their structural composition is, however, often very complex and hardly identifiable. The eligible way for obtaining definite structural interpretation of these systems appears the high-resolution solid-state nuclear magnetic resonance (ssNMR) spectroscopy. For this purpose the reliable tool - the ssNMR toolbox for comprehensive characterization of various pharmaceutical solids is described. The rigorous optimization of ssNMR techniques is carried out on enormous number of measured samples containing active pharmaceutical ingredients (APIs) with systems ranging from APIs formulated in solid dispersions to pure forms revealing extensive molecular disorder. In this study the influence of polymeric matrix on the creation of solid dispersion type susceptible for finely tuned controlled drug release is likewise discussed. The distinction between variable structural alignments of API molecules in 3D dimension of complicated pharmaceutical solids is allowed via simple strategy - factor analysis applied to hardly describable ssNMR spectra (13 C CP/MAS NMR and 19 F MAS NMR). The results of this ssNMR investigation contribute to better understanding of solid dispersion...
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Dynamical Behaviour of Matrix Proteins from Mason-Pfizer Monkey Virus
Srb, Pavel ; Lang, Jan (advisor) ; Žídek, Lukáš (referee) ; Brus, Jiří (referee)
Title: Dynamical behaviour of matrix proteins from Mason-Pfizer Monkey Virus Author: Pavel Srb Department: Department of Low temperature physics Supervisor: doc. RNDr. Jan Lang, PhD. Abstract: We studied the oligomeric properties of betaretroviral nonmyristoylated ma- trix protein (MA) and its R55F mutant from the Mason-Pfizer monkey virus in solution by means of NMR spectroscopy. We have proven that the wild- type (WT) MA forms oligomers in solution. The final model of oligomeriza- tion of the WT MA was derived by concerted use of chemical shift mapping and diffusion-ordered spectroscopy measured on a set of protein samples with varying concentrations. We found that the Mason-Pfizer monkey virus WT MA exists in a monomer-dimer-trimer equilibrium in solution. Further a combination of NMR relaxation measurements and advanced analysis of molecular dynamics simulation trajectory provided an unprecedentedly de- tailed insight into internal mobility of matrix proteins of the Mason-Pfizer monkey virus. Strong evidence have been obtained that the oligomerization capacity of the wild-type matrix protein is closely related to the enhanced dynamics of several parts of its backbone on a nanosecond time scale. In- creased flexibility has been observed for two regions: the loop between he- lices α2 and α3 and the C-terminal...
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Final report about research in Sokolov post mining sites in 2015 based on agreement between ENKI ops and Institute of Soil Biology BC CAS
Frouz, Jan ; Moradi, J. ; Mudrák, Ondřej ; Albrechtová, Jana ; Kučera, J. ; Kukla, J. ; Bednářová, E. ; Vindušková, O. ; Sebag, D. ; Cailleau, G. ; Brus, Jiří
The report brings main results of the research about soil and ecosystem recovery in post mining landscape near Sokolov based on agreement between ENKI ops and Institute of soil biology, BC CAS.
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