Thesis On Ubiquitin

Thesis On Ubiquitin-72
The thesis examines in detail the folding and unfolding processes of a number of proteins including hb SBD, DDLNF4, single and multi Ubiquitin.Using simplified coarse-grained off-lattice Go model and CD experiments we have shown the two-state behavior of hb SBD protein.

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A technology was developed known as Protac (Proteolysis Targeting Chimeric Molecule), that acts as a bridge, bringing together the SCF ubiquitin ligase with a protein target, resulting in its ubiquitination and degradation.

The Protac contains a peptide moiety at one end that is recognized by SCF that is chemically linked to the binding partner or ligand of the target protein.

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.

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.By proximity-dependent biotin identification (Bio ID), co-immunoprecipitation, and proximity-ligation assay (PLA), I identified the heat shock proteins HSC/HSP70 and HSP90 as novel Ch AT protein-interactors that are enriched in cells expressing mutant P17A/P19A-Ch AT.Pharmacological inhibition of these HSPs by treatment with the HSC/HSP70 inhibitors 2-phenylethynesulfonamide (PES) or VER-155008, or the HSP90 inhibitor 17-AAG reduced cellular Ch AT activity and solubility, and enhanced ubiquitination and proteasomal loss of Ch AT protein.Ph D thesis by Maksim Kouza defended at Institute of Physics Polish Academy of Sciences in 2009 (supervisor Prof. The enzyme choline acetyltransferase (Ch AT) mediates synthesis of the neurotransmitter acetylcholine required for cholinergic neurotransmission.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.Most proteins are targeted to the 26S proteasome by covalent attachment of a multiubiquitin chain.A key component of the enzyme cascade that results in attachment of the multiubiquitin chain to the target or labile protein is the ubiquitin ligase that controls the specificity of the ubiquitination reaction.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.


Comments Thesis On Ubiquitin

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