Thesis On Ubiquitin

Thesis On Ubiquitin-23
The first demonstration of the efficacy of Protac technology was the successful recruitment, ubiquitination, and degradation of the protein Methionine Aminopeptidase-2 (Met AP-2) through a covalent interaction between Met AP-2 and Protac.Subsequently, we demonstrated that Protacs could effectively ubiquitinate and degrade cancer-promoting proteins (estrogen and androgen receptors) through non-covalent interactions in vitro and in cells.

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Contrary to the standard temperature RE, the exchange is carried out between different forces (replicas).

Our method was successfully applied to study thermodynamics of a three-domain Ubiquitin.

It is currently unknown if this motif regulates Ch AT function.

In this thesis, I demonstrate that disruption of this proline-rich motif in mouse cholinergic SN56 cells reduces both the protein levels and cellular enzymatic activity of mutated P17A/P19A- and V18M-Ch AT.

Protein degradation is one of the tactics employed by the cell for irreversibly inactivating proteins.

In eukaryotes, ATP-dependent protein degradation in the cytoplasm and nucleus is carried out by the 26S proteasome.

This peak can not be encountered by the Go models in which the non-native interactions are neglected.

Our finding may stimulate further experimental and theoretical studies on this protein.

The cellular loss of mutant Ch AT protein appears to be a result of increased proteasome-dependent degradation due to enhanced Ch AT ubiquitination.

Using a novel fluorescent-biorthogonal pulse-chase protocol, I determined that the cellular protein half-life of P17A/P19A-Ch AT (2.2 h) is substantially reduced compared to wild-type Ch AT (19.7 h), and that proteasome inhibition by MG132 treatment increases the half-life and steady-state levels of Ch AT protein.


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