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National Repository of Grey Literature 2 records found  Search took 0.01 seconds. 
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...
Detailed record
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...
Detailed record

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