| dc.contributor.advisor | Chval, Zdeněk | |
| dc.contributor.author | Dvořáková, Kateřina | |
| dc.date.accessioned | 2021-12-03T06:56:11Z | |
| dc.date.available | 2021-12-03T06:56:11Z | |
| dc.date.issued | 2007 | |
| dc.date.submitted | 2007-05-15 | |
| dc.identifier.uri | https://dspace.jcu.cz/handle/20.500.14390/17316 | |
| dc.description.abstract | Interakce kovových iontů významným způsobem ovlivňují strukturu a funkci nukleových kyselin a proteinů. Přibližně polovina enzymů obsahuje ionty kovů jako kofaktory a většina ribozymů nemůže správně fungovat bez přítomnosti iontů kovů. Nejčastěji vyskytujícími se kovy v proteinech jsou Ca2+, Mg2+ a Zn2+. Tato práce je zaměřena na analýzu rentgenových struktur biomolekul obsahujících Zn2+ ionty z hlediska jejich vaznosti. Získaná data jsou následně porovnána s obdobnými daty pro vaznost Mg2+ iontů na biomolekuly. | cze |
| dc.format | 51 | |
| dc.format | 51 | |
| dc.language.iso | cze | |
| dc.publisher | Jihočeská univerzita | cze |
| dc.rights | Bez omezení | |
| dc.subject | Zinek | cze |
| dc.subject | koordinační vrstva | cze |
| dc.subject | proteiny | cze |
| dc.subject | nukleové kyseliny | cze |
| dc.subject | Zinc | eng |
| dc.subject | proteins | eng |
| dc.subject | nucleic acids | eng |
| dc.title | Interakce Zn2+ iontů s proteiny a nukleovými kyselinami | cze |
| dc.title.alternative | Interactions of Zn2+ ions with proteins and nucleic acids | eng |
| dc.type | bakalářská práce | cze |
| dc.identifier.stag | 7003 | |
| dc.description.abstract-translated | Interaction of Zn2+ ions with proteins and nucleic acids
Zinc is an important metal in biological systems. It is a strong Lewis acid, forms a stable Zn2+ ion and can exist in several coordination geometries. Zinc is required for the activity of more than 300 enzymes. In proteins zinc can either participate directly in chemical catalysis or can be important for maintaining protein structure and stability.
In this work a dataset of high quality (resolution better than 3 Ǻ) crystal structures deposited in the Protein Data Bank on internet have been examined to identify typical zinc binding sites and to establish their coordination geometries. Totally 135 zinc binding sites found in 74 structures have been analyzed.
The most frequent coordinating atoms are sulphur in cystein, NE2 and ND1 nitrogens in histidine followed by oxygen atoms in carboxylates of aspartic and glutamic acids. 67% of zinc binding sites were found to be four-coordinated with tetrahedral coordination geometry. In contrast Mg2+ cations show a clear preference to bind to oxygen atoms and to form octahedral cavities. We have not found any structure with a direct zinc coordination to DNA except the 1ZQT structure which was however excluded due to its low resolution (> 3 Å). Similarly only three zinc binding sites have been found in RNA structures which were however determined in the protein free environment. All other zinc binding sites have been located in proteins even in the presence of the nucleic acids. | eng |
| dc.date.accepted | 2007-06-22 | |
| dc.description.department | Zdravotně sociální fakulta | cze |
| dc.thesis.degree-discipline | Biofyzika a zdravotnická technika | cze |
| dc.thesis.degree-grantor | Jihočeská univerzita. Zdravotně sociální fakulta | cze |
| dc.thesis.degree-name | Bc. | |
| dc.thesis.degree-program | Biofyzika | cze |
| dc.description.grade | Dokončená práce s úspěšnou obhajobou | cze |
| dc.contributor.referee | Kabeláč, Martin | |
| dc.description.defence | Obhajoba bakalářské práce: Prezentace výsledků byla dobře připravena.
Klasifikace: Výborně | cze |
