| dc.date.accessioned |
2017-06-06T13:21:21Z |
und |
| dc.date.accessioned |
2017-10-24T12:19:34Z |
|
| dc.date.available |
2017-06-06T13:21:21Z |
und |
| dc.date.available |
2017-10-24T12:19:34Z |
|
| dc.date.issued |
2017-06-06T13:21:21Z |
|
| dc.identifier.uri |
http://radr.hulib.helsinki.fi/handle/10138.1/6068 |
und |
| dc.identifier.uri |
http://hdl.handle.net/10138.1/6068 |
|
| dc.title |
Multi-dimensional nuclear magnetic resonance spectroscopy techniques as tools for probing the protein-protein interaction of filamin A domains 20-21 with migfilin |
en |
| ethesis.department.URI |
http://data.hulib.helsinki.fi/id/c2dd677c-da9c-4011-94b0-27b1585ac1cb |
|
| ethesis.department |
Kemiska institutionen |
sv |
| ethesis.department |
Biocenter Finland, Institute of Biotechnology |
sv |
| ethesis.department |
Department of Chemistry |
en |
| ethesis.department |
Biocenter Finland, Institute of Biotechnology |
en |
| ethesis.department |
Kemian laitos |
fi |
| ethesis.department |
Biocenter Finland, Institute of Biotechnology |
fi |
| ethesis.faculty |
Matematisk-naturvetenskapliga fakulteten |
sv |
| ethesis.faculty |
Matemaattis-luonnontieteellinen tiedekunta |
fi |
| ethesis.faculty |
Faculty of Science |
en |
| ethesis.faculty.URI |
http://data.hulib.helsinki.fi/id/8d59209f-6614-4edd-9744-1ebdaf1d13ca |
|
| ethesis.university.URI |
http://data.hulib.helsinki.fi/id/50ae46d8-7ba9-4821-877c-c994c78b0d97 |
|
| ethesis.university |
Helsingfors universitet |
sv |
| ethesis.university |
University of Helsinki |
en |
| ethesis.university |
Helsingin yliopisto |
fi |
| dct.creator |
Rodić, Nebojša |
|
| dct.issued |
2017 |
|
| dct.language.ISO639-2 |
eng |
|
| dct.abstract |
Ever since its discovery over four decades ago, filamin A has been at the forefront of research interests in the field of cytoskeletal proteins. A member of the filamin family, filamin A cross-links actin microfilaments into three-dimensional networks and has an important role in many critical processes happening within cells, including but not limited to cell motility, signal transduction, maintaining cell shape. These roles are reflected in the fact that a multitude of filamin A binding partners were found over the years. We used novel multi-dimensional nuclear magnetic resonance techniques to investigate the possible binding of filamin A and migfilin, a protein whose role in the organism is not well understood. The results of the research suggest that strong binding between filamin A and migfilin takes place. The location within the fragment of filamin A where migfilin binds has been determined to enable further research into the structure of the complex the two proteins form. |
en |
| dct.language |
en |
|
| ethesis.language.URI |
http://data.hulib.helsinki.fi/id/languages/eng |
|
| ethesis.language |
English |
en |
| ethesis.language |
englanti |
fi |
| ethesis.language |
engelska |
sv |
| ethesis.thesistype |
pro gradu-avhandlingar |
sv |
| ethesis.thesistype |
pro gradu -tutkielmat |
fi |
| ethesis.thesistype |
master's thesis |
en |
| ethesis.thesistype.URI |
http://data.hulib.helsinki.fi/id/thesistypes/mastersthesis |
|
| ethesis.degreeprogram |
Advanced Spectroscopy in Chemistry |
en |
| dct.identifier.urn |
URN:NBN:fi-fe2017112251404 |
|
| dc.type.dcmitype |
Text |
|
