Molecular characterisation of DDX49
DEAD box proteins are the largest family of RNA helicases, composed of 37 members and are involved in the central and essential physiological aspects of RNA metabolism. They are characterised by a structurally highly conserved helicase core, composed of 2 RecA like domains connected via a flexible l...
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| Format: | Thesis (University of Nottingham only) |
| Language: | English |
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2024
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| Online Access: | https://eprints.nottingham.ac.uk/78447/ |
| _version_ | 1848801082962083840 |
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| author | Kapllanaj, Fiorela |
| author_facet | Kapllanaj, Fiorela |
| author_sort | Kapllanaj, Fiorela |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | DEAD box proteins are the largest family of RNA helicases, composed of 37 members and are involved in the central and essential physiological aspects of RNA metabolism. They are characterised by a structurally highly conserved helicase core, composed of 2 RecA like domains connected via a flexible linker and flanked by the N and C terminus domains of the protein, as shown in figure 1.1 (Donsbach and Klostermeier, 2021).
The interplay of the 9 conserved motifs of the helicase core gives these family of proteins the ability to hydrolyse ATP, bind and unwind RNA duplexes. The characteristic Motif II, also known as the Asp-Glu-Ala-Asp (D-E-A-D) motif, together with motif Q, I and VI carry out ATP binding and hydrolysis, as shown in figure 1.1 (Linder and Jankowsky, 2011). |
| first_indexed | 2025-11-14T21:01:48Z |
| format | Thesis (University of Nottingham only) |
| id | nottingham-78447 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T21:01:48Z |
| publishDate | 2024 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-784472024-07-16T04:40:40Z https://eprints.nottingham.ac.uk/78447/ Molecular characterisation of DDX49 Kapllanaj, Fiorela DEAD box proteins are the largest family of RNA helicases, composed of 37 members and are involved in the central and essential physiological aspects of RNA metabolism. They are characterised by a structurally highly conserved helicase core, composed of 2 RecA like domains connected via a flexible linker and flanked by the N and C terminus domains of the protein, as shown in figure 1.1 (Donsbach and Klostermeier, 2021). The interplay of the 9 conserved motifs of the helicase core gives these family of proteins the ability to hydrolyse ATP, bind and unwind RNA duplexes. The characteristic Motif II, also known as the Asp-Glu-Ala-Asp (D-E-A-D) motif, together with motif Q, I and VI carry out ATP binding and hydrolysis, as shown in figure 1.1 (Linder and Jankowsky, 2011). 2024-07-16 Thesis (University of Nottingham only) NonPeerReviewed application/pdf en cc_by_nc_nd https://eprints.nottingham.ac.uk/78447/1/Kapllanaj_Fiorela_20218948_Mres_Thesis.pdf Kapllanaj, Fiorela (2024) Molecular characterisation of DDX49. MRes thesis, University of Nottingham. DEAD box helicases; Enzymatic activates; Mutagenesis; DNA binding; DNA unwinding; Nuclease activities |
| spellingShingle | DEAD box helicases; Enzymatic activates; Mutagenesis; DNA binding; DNA unwinding; Nuclease activities Kapllanaj, Fiorela Molecular characterisation of DDX49 |
| title | Molecular characterisation of DDX49 |
| title_full | Molecular characterisation of DDX49 |
| title_fullStr | Molecular characterisation of DDX49 |
| title_full_unstemmed | Molecular characterisation of DDX49 |
| title_short | Molecular characterisation of DDX49 |
| title_sort | molecular characterisation of ddx49 |
| topic | DEAD box helicases; Enzymatic activates; Mutagenesis; DNA binding; DNA unwinding; Nuclease activities |
| url | https://eprints.nottingham.ac.uk/78447/ |