ࡱ> #% !"U@ bjbj  8 $B 8jZ p  7777777$l9R;b7 ^ 7 7@@@  7@7@&@f3%#' N h* %7708%6 <" <,#'#'^ <' "@*> 77d *  Molecular dynamics simulation of temperature-induced unfolding of prion protein  Thesis in part fulfilment of MSc degree by Richard Wilson Supervisor: Dr. Andreas Kukol, Biological Sciences In collaboration with Dr. Teresa Pinheiro, Biological Sciences Funded by the  SHAPE \* MERGEFORMAT  Summary This document is a report of an eight week project performed as part of the first (MSc) year of the MOAC interdisciplinary life sciences doctoral training programme at TV University. MOAC stands for molecular organisation and assembly in cells. The context of the project is research aiming at a better understanding of transmissible spongiform encephalopathies, neurodegenerative diseases in which the infectious agent is a misfolded protein called a prion. Dr Teresa Pinheiro and her group are focussing on protein folding; fluorescence techniques are used to monitor the process of folding. Mutant prions have been engineered with improved fluorescence characteristics compared to the wild type. However, the mutants have elevated unfolding temperatures and so may not faithfully reproduce wild type behaviour. The aim of this project is to gain more information about the difference in unfolding temperature. The project is a molecular dynamics simulation study of prion protein unfolding using the GROMACS package. The mutant version of prion with the most different temperature characteristic was chosen to compare with the wild type in silico. To match the experimental environment, each type of prion was simulated in water solution at pH7 for 12ns at 4 temperatures: 298K, 372K, 440K and 500K. Trajectories recording the series of positions of the protein at set time intervals in the simulation were obtained for each simulation run and the results analysed. Although it has been impossible to determine more than a range for the unfolding temperatures, the data indicate that the mutant is more resistant to unfolding and, though its unfolding behaviour is similar to the wild type, there are intriguing differences. Precise determination of unfolding temperatures, firm evidence of any significant differences in unfolding behaviour and detailed explanation of the difference require further work.  PAGE 1 &(1FTUVW\}~     ) * + , - ȽȪ~~zrnr`XrjQh!Ujh!UmHnHuh!jh!UhqFh.h 4ha7h)vhd=WhCh7hQh)h}-hzejh.Uhzeho4CJ0aJ0hzehRGCJ0aJ0hzehCCJ0aJ0hzeh CJ0aJ0h&oCJ0aJ0h >CJ(aJ("jh CJ(UaJ(mHnHu"TV   6 2 $a$gd/r$a$gdmgdgdagdk&$a$gddp$a$gdQ$a$gdC$a$gdRG- . 5 6 ; [ j ~   0 2 D P Y Z d  , - : I K 1 i j k n o hXhmhIh}hV(Whx:%hmKDhhu hC hPOh6@ht9hThq<]h9vh$h7haVhRIhgh3l hohahSha5CJ aJ ho48    / 7 = D K T U '+;?ATVs{)C쿻賿웗hhchhlshhDFh#h0h|hKq<h- hIhfh h%b6h%bh ]Qhx:%hRRh"Wh C?hXhJh6hPOhmh}uh9"0AE`sw˺h0JmHnHu h0Jjh0JUh hhhj2hThhhlshhhchR\@ 00&P 1hP:p. 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