So uh, does it not freak you out that there are things that look like worms that

move in your entire body at the molecular level? Come on, look at that first picture, it looks like a deadly spirochaette or something freaky

Post Translation Modification

So uh, does it not freak you out that there are things that look like worms that move in your entire body at the molecular level? Come on, look at that first picture, it looks like a deadly spirochaette or something freaky

Usually protein synthesis yields enzyme precursors instead of fully functional enzymes. Most newly synthesized proteins undergo modifications first before becoming functional in different body cells.

Secreted Proteins and Membrane Proteins

Proteins will either be secreted by the cell Or become a membrane protein All synthesized proteins have signal sequence or signal peptide (of 13-36 predominantly hydrophobic residues)

Proteolytic Cleavage
Cleavage/removal of an amino acid at a peptide bond. Hydrolysis of peptide bonds, unlinking some parts of the polypeptide Enzyme: Protease May lead to protein activation, inhibition or destruction Ex. Preproprotine of insulin Preproprotine > proinsulin > insuling

Acetylation
Addition of acetyl group (e.g. methyl) to N-terminus of polypeptide or to its lysine residue Catalyzing enzyme: acetyltransferase (NATs or HAT) 80-90% of human proteins are N-acetylated Histones are lysine acytelated Essential for signalling

Phosphorylation
Addition of phosphate group to the polypeptide Usually to serine>threonine>tyrosine and histidine. Catalyzing enzyme: Protein kinase ATP + protein <> phosphoprotein + ADP Most common protein modification, important for regulatory mechanism. ex. Phosphorylation of glycogen synthase and glycogen phosphorylase in hepatocytes in response to glucagon release of pancrease > Increased hepatic glucose delivery to blood.

Sulfation
Permanent addition of sulfate group to polypeptide Specifically to tyrosine Catalyzing enzyme: tyrosylprotein sulfotransferase (TPST) Sulfate donor: PAPS Adds stability to protein, strengthening protein-protein interactions Secreted proteins and extracellular parts of membrane proteins that pass through golgi apparatus may undergo sulfation.

Amidation
Addition of an amide to C-terminus of peptide Commonly done to peptide hormones Gives structural stability and resistance to hydrolysis

Ubiquitinylation
Addition of Ubiquitin via an isopeptide bond (not on main chain) Ubiquitin small (76 AA) regulatory protein found in almost all tissues. Varying function depending on length Addition leads to tagging of protein for destruction by the proteosome organelle Or directed to other parts of the cell.

Glycosylation
Attachment of sacharrides to polypeptides Creates more structural stability or new functions to the protein. Proper anchoring Cell recognition Protein folding Types: N-glycosylation O-glyocsylation C-mannosylation GPI anchor

So uh, does it not freak you out that there are things that look like worms that move in your entire body at the molecular level? Come on, look at that first picture, it looks like a deadly spirochaette or something freaky

END

So uh, does it not freak you out that there are things that look like worms that move in your entire body at the molecular level? Come on, look at that first picture, it looks like a deadly spirochaette or something freaky