Lecture 12.docx

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Department
Biological Sciences
Course
BIO SCI M114
Professor
Alexander Mc Pherson
Semester
Spring

Description
Lecture 12 02/18/2014 Paper: 1. Due Mar. 6 Mar. 11 is okay too 2. Final on Mar. 13 post translational modificaitons some are reversible Phosphorylation Turning on/off metabolism events Proteolysis Trypsin is cleaved then is activated in the gut, synthesized by liver  Pituitary gland:: most peptides that come out are cleaved Insulin: Preproinsulin, proinsulin, mature insulin know the events Has signal sequence, to cross membranes (Preproinsulin) Proinsulin has di­sulfide bonds and signal sequence is cleaved The disulfide bonds become inter­chain bonds in insulin Requires Zinc to be active Phosphorylation occurs usually at   Ser, Thr, Tyr   (common)   Arg, Lys, His happen sometimes too (but are not phospho­ester bonds) Glycosylation, ogliosacharides are attached to protein by asn, ser or thr Purpose: exterior of cells, recognition sites for cells Antibodies! Antigens on the surface of cells Make the molecule bigger so it does not get filtered out Ribonuclease A (amphisens, primary AA) Rib. B has glycosylation Make proteins soluble ! Passport hypothesis Glycosylation has a particular sequence (branced/linear) As glycos. Proteins circulate, one of the sugars get chopped off from the liver, and as the oglio. Gets short  enough, the liver degrades the protein N­linked Asn­X­Ser (Gluc. N­ Actyl) O­Linked Ser­Gly­X­Gly Usually the sugar chain has no structure, because it is in solution and hydrolyzed Cytoskeletal fibers Globular proteins that polymerize to form long structures Membrane proteins 40% proteins are membrane proteins 90% of all important proteins
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