20.500.12556/DKUM-72042 Maksimalna produkcija entropije in maksimalna shannonova informacijska entropija v encimski kinetiki Maximum entropy production and maximum shannon information entropy in enzyme kinetics Princip maksimalne produkcije entropije je osrednji optimizacijski princip neravnovesne termodinamike. Princip je dobro raziskan in uveljavljen v sistemih, kjer je zveza med silami in tokovi linearna. Za sisteme, kjer je ta zveza nelinearna pa princip še ni povsem uveljavljen. Primer sistema, kjer je zveza med silami in tokovi nelinearna, so encimske reakcije. V tem magistrskem delu z uporabo principa maksimalne produkcije entropije analiziramo encimsko reakcijo, ki jo poganja encim trioza-fosfat izomeraza, ki je pomemben člen v procesu glikolize in s tem pri proizvodnji energije v večini organizmov. Encim poganja reverzibilno reakcijo v kateri pretvarja substrat dihidroksi acetonfosfat v gliceraldehid-3-fosfat preko vmesnega člena iz skupine enediolov. Z upoštevanjem zakona o ohranitvi mase sistema, ohranitvi encima in fiksne ravnovesne konstante reakcije pokažemo, da v neravnovesnem stacionarnem stanju sistema obstaja maksimum produkcije entropije v odvisnosti od poljubno izbrane kinetične konstante encima. Pokazano je tudi, da v stanju z maksimalno produkcijo entropije soobstajata maksimuma Shannonove informacijske entropije in kinetične fleksibilnosti, kar pomeni, da je stanje z maksimalno produkcijo entropije hkrati tudi najverjetnejše stacionarno stanje, v katerem je encim najfleksibilnejši. Tako napovedane optimalne kinetične konstante encima trioza-fosfat izomeraza primerjamo z eksperimentalno določenimi vrednostmi iz literature in s teoretičnimi napovedmi, ki so jih podali drugi raziskovalci z uporabo svojih optimizacijskih metod. The maximum entropy production principle is an optimization principle in non-equilibrium thermodynamics. The principle is well established and accepted for systems in which the relationship between fluxes and forces is linear. However, it is still not clear if the principle is valid for systems with non-linear force-flux relationships. Enzyme reactions are examples of such non-linear systems. In this master thesis we apply the maximum entropy production principle to the reaction catalysed by the enzyme triosephosphate isomerase which is an important enzyme in the glycolysis process and thus for energy production in most organisms. The enzyme catalyses the reversible interchange of dihydroxy acetonphosphate to glyceraldehyde-3-phosphate with an enediol intermediate. Under the constraints of mass conservation, enzyme conservation and a fixed equilibrium constant of the reaction we show that a maximum in entropy production in a steady state exists as a function of an arbitrary chosen enzyme rate constant. Moreover, we show that in the state of maximum entropy production maxima of Shannon information entropy and kinetic flexibility coexist. This means that the steady state with a maximum in entropy production is also the most probable steady state in which the enzyme is most flexible. We compare the optimal enzyme rate constants calculated by this method with experimentally observed values as well as with values from the literature published by other authors. trioza-fosfat izomeraza encimska kinetika produkcija entropije informacijska entropija kinetična fleksibilnost triosephosphate isomerase enzyme kinetics entropy production information entropy kinetic flexibility true true false [M. Šterk] Slovenski jezik Angleški jezik Magistrsko delo/naloga 2018-09-07 13:42:09 2021-02-04 12:32:52 2022-08-01 21:54:00 2021-02-05 03:23:27 2018 0 Maribor 0 0000-00-00 NiDoloceno NiDoloceno NiDoloceno 0000-00-00 0000-00-00 0000-00-00 536.75(043.2) 24106504 URN:SI:UM:DK:QMQNYB2M MAG_Sterk_Marko_2018.pdf MAG_Sterk_Marko_2018.pdf 1 1683EA9F922C6931E96FB30308A473BC 2f4c6b008ba70730ae561ec8e334536daa4abee39c94f002b6ffbce7a6b9c17a 4678f22e-7c10-11eb-bb7a-00155d0001ca 20.500.12556/dkum/fae737f0-74dc-469e-923d-f91d8ab050e6 https://dk.um.si/Dokument.php?lang=slv&id=128933 Fakulteta za naravoslovje in matematiko 0 0 0