Lecture 1 - 5 Flashcards
What is post translational modification?
- covalent addition/ cleavage of proteins after protein biosynthesis = occurs on the amino-acid chain or at a terminal
How do cells become pluripotent stem cells?
modify transcription factors within the cells and cause fully formed cells to revert/reprogram into pluripotent stem cells
What are the key types of post-translational modifications of proteins?
- phosphorylation
- glycosylation
- acetylation
- methylation
What does cleavage refer to?
in terms of adding nucleases and restriction enzymes where the DNA is cut
How is insulin produced in terms of cleavage?
- protein being produced by ribosome and fed through membrane into interstitial space.
- produces one large primary structure with parts that need to be cut away
- post translational modification is produced
- protein exported into golgi vessels to be cleaved
- unwanted peptide parts are removed
- produce a smaller protein product which can act as insulin
What is the function of adding new functional groups to proteins?
enable cell signaling and the cell to react specifically and rapidly to events
What is phosphorylation?
the addition of a phosphate group to the protein, which changes its activity
What are protein kinases?
enzymes that catalyze the transfer of a phosphate group from a high-energy donor molecule to a specific substrate-phosphorylation
How do protein kinases transfer a phosphate group to a protein?
Take ATP and remove the phosphate from it and knock the hydrogen off of the hydroxyl group and add a phosphate to it
What is phosphatases?
enzyme that catalyse the removal of a phosphate group from a substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group
What is the regulation of glycogen breakdown by phosphorylation?
- pathway initiated by epinephrine binding to its receptor and cAMP binding to cAMP-dependent protein kinase.
- signal transmitted to its intracellular target by the sequential action of protein kinases
What is glycosylation?
when a carbohydrate is covalently bound to a functional group on a protein via a glycosidic bond
what is the function of glycosylation?
- help correct folding of protein
- increase protein stability
- immune response
What are the 5 types of glycosylation?
- N-linked = glycan bind to amino group of asparagine
- O-linked = monosaccharides bind to hydroxyl group serine or threonine
- Glypiation = glycan core links a phospholipid and a protein
- C-linked = mannose binds to the indole ring of trytophan
- Phosphoglycosylation = glycan binds to serine via phosphodiester bond
What are the two types of acetylation?
- N-terminal
- Lysine acetylation
What is the role of N-terminal acetyltransferases (NATs)?
NATS transfer an acetyl group from acetyl-coenzyme A (AC-CoA) to the alpha amino group o f the first amino acid residue of the protein