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National Repository of Grey Literature 2 records found  Search took 0.01 seconds. 
Měření C-13 NMR relaxací karbonylových skupin v proteinech
 Grocký, Marián ; Hrabal, Richard (referee)
Title: Measurement of 13 C NMR relaxation of Carbonyl Groups in Proteins Author: Marián Grocký Department: Department of Low Temperature Physics Supervisor: RNDr. Jan Lang, PhD. Supervisor's email address: Jan.Lang@mff.cuni.cz Abstract: I have investigated measurement methods of 13 C NMR longitudial and transversal relaxation constants in proteins labeled by 13 C, 15 N. The Mason-Pfizer Matrix protein (M-PMV) has been studied in it's wild form (WT) and mutated form (R55F) by these methods in order to reveal its dynamics. It has been known that point mutation of arginine for phenylalanine at the 55th position of matrix protein changes virus's life cycle. Reproduction of M-PMV than resembles HIV virus reproduction. Nitrogen T1, T2 and NOE relaxation experiments have also been carried out. All relaxation data were used for Lipari-Szabó model-free approach in order to get and compare carbonyl and amide group motion parameters. There has been found a high similarity between carbonyl and nitrogen motion parameters within WT protein. Nitrogen data of R55F protein approved higher mobility of particular sequences in that protein, which is assumed to be responsible for changes in mutant's life cycle. Both carbonyl and nitrogen data significantly enlarged our current knowledge of dynamics of both WT and R55F...
Detailed record
Měření C-13 NMR relaxací karbonylových skupin v proteinech
 Grocký, Marián ; Hrabal, Richard (referee)
Title: Measurement of 13 C NMR relaxation of Carbonyl Groups in Proteins Author: Marián Grocký Department: Department of Low Temperature Physics Supervisor: RNDr. Jan Lang, PhD. Supervisor's email address: Jan.Lang@mff.cuni.cz Abstract: I have investigated measurement methods of 13 C NMR longitudial and transversal relaxation constants in proteins labeled by 13 C, 15 N. The Mason-Pfizer Matrix protein (M-PMV) has been studied in it's wild form (WT) and mutated form (R55F) by these methods in order to reveal its dynamics. It has been known that point mutation of arginine for phenylalanine at the 55th position of matrix protein changes virus's life cycle. Reproduction of M-PMV than resembles HIV virus reproduction. Nitrogen T1, T2 and NOE relaxation experiments have also been carried out. All relaxation data were used for Lipari-Szabó model-free approach in order to get and compare carbonyl and amide group motion parameters. There has been found a high similarity between carbonyl and nitrogen motion parameters within WT protein. Nitrogen data of R55F protein approved higher mobility of particular sequences in that protein, which is assumed to be responsible for changes in mutant's life cycle. Both carbonyl and nitrogen data significantly enlarged our current knowledge of dynamics of both WT and R55F...
Detailed record

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