Characterisation And Crystallisation Of Deptor

dc.contributor.author	Yeap, Kean Heng
dc.date.accessioned	2022-06-30T09:10:10Z
dc.date.available	2022-06-30T09:10:10Z
dc.date.issued	2021-02
dc.description.abstract	The mechanistic target of rapamycin (mTOR) signalling pathway integrates wide varieties of nutrients to regulate important cellular processes related to cell growth. mTOR is a huge serine/threonine protein kinase and exists in two distinct complexes, mTORC1 and mTORC2. DEPTOR is an endogenous inhibitor of mTOR and consists of two DEP domains in tandem arrangement and a PDZ domain. The Escherichia coli expression system was used for cloning and expression experiments. Here, besides the full-length protein, various truncated mutants were designed as well to gain insights into the characteristics and architectures of the protein. Four truncated mutants were constructed to represent the first DEP domain (DEP1), the second DEP domain (DEP2), both DEP domains (DEP12) and the PDZ domain. DEPTOR, DEP1, DEP2 and DEP12 were expressed as soluble proteins but PDZ was insoluble.	en_US
dc.identifier.uri	http://hdl.handle.net/123456789/15516
dc.language.iso	en	en_US
dc.publisher	Universiti Sains Malaysia	en_US
dc.subject	Characterisation And Crystallisation	en_US
dc.subject	Deptor	en_US
dc.title	Characterisation And Crystallisation Of Deptor	en_US
dc.type	Thesis	en_US

Now showing 1 - 1 of 1