| dc.contributor.advisor | Kutá Smatanová, Ivana | |
| dc.contributor.author | Doleželová, Katsiaryna | |
| dc.date.accessioned | 2023-03-07T11:03:20Z | |
| dc.date.available | 2023-03-07T11:03:20Z | |
| dc.date.issued | 2019 | |
| dc.date.submitted | 2019-03-11 | |
| dc.identifier.uri | https://dspace.jcu.cz/handle/20.500.14390/40822 | |
| dc.description.abstract | Disertační práce se věnuje analýze 3D struktur haloalkan dehalogenáz DpcA z Psychrobacter cryohalolentis K5 a DmxA z Marinobacter sp ELB17, které jsou jsou vhodné pro různé biologické aplikace. | cze |
| dc.format | I-XIII, 1-165 | |
| dc.format | I-XIII, 1-165 | |
| dc.language.iso | eng | |
| dc.publisher | Jihočeská univerzita | cze |
| dc.rights | Bez omezení | |
| dc.subject | Krystallizace | cze |
| dc.subject | makromolekulární krystalografie | cze |
| dc.subject | strukturní charakterizace | cze |
| dc.subject | funkce proteinu | cze |
| dc.subject | haloalkan dehalogenázy | cze |
| dc.subject | enzymy | cze |
| dc.subject | biotechnologické využití | cze |
| dc.subject | haloalkane dehalogenases | eng |
| dc.subject | alpha/beta-hydrolase | eng |
| dc.subject | DpcA | eng |
| dc.subject | Psychrobacter cryohalolentis K5 | eng |
| dc.subject | DmxA | eng |
| dc.subject | Marinobacter sp ELB17 | eng |
| dc.subject | X-ray crystallography | eng |
| dc.subject | crystallization | eng |
| dc.subject | 3D structure | eng |
| dc.subject | protein function | eng |
| dc.subject | biotechnology | eng |
| dc.subject | biodegradation | eng |
| dc.title | Krystalografický
studium
biotechnologicky atraktivních haloalkan dehalogenáz
DpcA a DmxA | cze |
| dc.title.alternative | Crystallographic study of biotechnologically attractive haloalkane dehalogenases
DpcA and DmxA | eng |
| dc.type | disertační práce | cze |
| dc.identifier.stag | 28067 | |
| dc.description.abstract-translated | Since 1991, when the first haloalkane dehalogenase (HLD) from Xanthobacter autotrophicus GJ10 was described, nearly 20 HLDs have been characterized biochemically and fourteen HLDs were analysed structurally. These enzymes belong to alpha/beta-hydrolases and, owing to their ability to bring about the hydrolytic conversion of toxic halogenated compounds, are a source of broad biotechnological applications. DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17 are among them. Although their overall structures are quite similar to other HLD members, they possess several unique properties. Information on their 3D structure may significantly contribute to the understanding of protein function. DpcA and DmxA structures will allow us to gain insights into structural determinants of specificity and stability. This thesis aims to elucidate the tertiary and quaternary structures of these enzymes using of X-ray crystallography. | eng |
| dc.date.accepted | 2019-06-06 | |
| dc.description.department | Přírodovědecká fakulta | cze |
| dc.thesis.degree-discipline | Biofyzika | cze |
| dc.thesis.degree-grantor | Jihočeská univerzita. Přírodovědecká fakulta | cze |
| dc.thesis.degree-name | Ph.D. | |
| dc.thesis.degree-program | Biofyzika | cze |
| dc.description.grade | Dokončená práce s úspěšnou obhajobou | cze |
| dc.contributor.referee | Kolenko, Petr | |
| dc.contributor.referee | Kužel, Radomír | |
| dc.contributor.referee | Nemčovičová, Ivana | |
