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master's thesis
Drevni proteini kao termički stabilniji analozi postojećih proteina
Zagreb: University of Zagreb, Faculty of Science, 2017. urn:nbn:hr:217:702721
Viher, Marija
University of Zagreb
Faculty of Science
Department of Chemistry

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Viher, M. (2017). Drevni proteini kao termički stabilniji analozi postojećih proteina (Master's thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:702721

Viher, Marija. "Drevni proteini kao termički stabilniji analozi postojećih proteina." Master's thesis, University of Zagreb, Faculty of Science, 2017. https://urn.nsk.hr/urn:nbn:hr:217:702721

Viher, Marija. "Drevni proteini kao termički stabilniji analozi postojećih proteina." Master's thesis, University of Zagreb, Faculty of Science, 2017. https://urn.nsk.hr/urn:nbn:hr:217:702721

Viher, M. (2017). 'Drevni proteini kao termički stabilniji analozi postojećih proteina', Master's thesis, University of Zagreb, Faculty of Science, accessed 23 April 2024, https://urn.nsk.hr/urn:nbn:hr:217:702721

Viher M. Drevni proteini kao termički stabilniji analozi postojećih proteina [Master's thesis]. Zagreb: University of Zagreb, Faculty of Science; 2017 [cited 2024 April 23] Available at: https://urn.nsk.hr/urn:nbn:hr:217:702721

M. Viher, "Drevni proteini kao termički stabilniji analozi postojećih proteina", Master's thesis, University of Zagreb, Faculty of Science, Zagreb, 2017. Available at: https://urn.nsk.hr/urn:nbn:hr:217:702721

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Metadata
TitleDrevni proteini kao termički stabilniji analozi postojećih proteina
Title (english)Ancestral proteins as thermostable analogues of extant proteins
AuthorMarija Viher
MentorMarko Močibob (mentor)
Committee memberMarko Močibob (predsjednik povjerenstva)
Committee memberMarijana Đaković (član povjerenstva)
Committee memberIvan Kodrin (član povjerenstva)
Committee memberIta Gruić Sovulj (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Chemistry)
Zagreb
Defense date and country2017-09-25, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
Aminoacil-tRNA-sintetaze kataliziraju spajanje aminokiseline s pripadnom tRNA. Leucil-tRNA-sintetaza sadrži dodatnu domenu za popravak pogreške za hidrolizu nepripadno sparenih supstrata. Računalno rekonstruirani drevni proteini često su termički stabilniji od proteina iz kojih su izvedeni. Međutim, do sada ih se istraživalo zbog proučavanja mehanizama evolucije, a ne zbog primjene njihove termičke stabilnosti. Predmet ovoga rada su drevna leucil-tRNA-sintetaza i njezina mutirana inačica s inaktiviranom domenom za popravak. Termička stabilnost drevne leucil-tRNA-sintetaze ispitana je dvjema različitim metodama: diferencijalnom pretražnom fluorimetrijom i mjerenjem aktivnosti enzima pri povišenoj temperaturi. Određeni su njezini kinetički parametri u uvjetima ustaljenog i predustaljenog stanja. Drevna leucil-tRNA-sintetaza je termostabilnija od leucil-tRNA-sintetaze iz E. coli, a enzimi su identični u reakcijama aktivacije, prijenosa aminokiseline i popravka pogreške. Drevni enzimi stoga mogu pronaći primjenu kao termički stabilniji analozi postojećih proteina u uvjetima gdje je poželjna veća stabilnost enzima.
Abstract (english)
Aminoacyl-tRNA synthetases catalyse coupling of amino acids with their cognate tRNAs. Leucyl-tRNA synthetase has additional editing domain in which hydrolysis of misactivated amino acids takes place. Inferred ancestral proteins often show greater thermostability than their extant descendant proteins. However, until now they were used in evolution mechanism research and not due to application of their thermal properties. Subject of this thesis are ancestral leucyl-tRNA synthetase and its mutant with inactivated editing domain. Thermostability of ancestral leucyl-tRNA-synthetase was monitored with two different methods: differential scanning fluorimetry and enzyme activity measurement. Its kinetical parameters were determined with steady state and pre-steady state kinetics. Ancestral leucyl-tRNA synthetase is more thermostable than E. coli leucyl-tRNA synthetase and both enzymes are kinetically identical in reactions of amino acid activation, transfer on tRNA and editing. Therefore, ancestral enzymes can be used as thermostable analogues of extant proteins in conditions that ask for greater stability.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:702721
Study programmeTitle: Graduate university studies in chemistry; specializations in: Research programme
Course: Research programme
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra kemije (magistar/magistra kemije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
RepositoryRepository of the Faculty of Science
Created on2017-10-17 16:39:07

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