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bio lec8-11 PART1 - the SRP is a riboptn it fix at the...

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- the SRP is a riboptn - it fix at the different places of the ribosome’s which is needed to bring in all these elongation factor which transport tRNA for making ptn so it stop the ptn synthesis in that state - so the transfer for this ptn depend on the start transfer signal recognize by the SRP - and for the transmem ptn need a second complex the translocator has to recognize the start transfer signal and the stop transfer signal - and this lead to stop of the transfer and the signal peptidase cleave the stop the transfer signal and leaving this in the lateral way to the mem “the translocator open laterally” the orientation of he ptn is depending on the charged of the surrounding aa and this is the reason why in this case 2 start signal here is located in the neighborhood so the start transfer start again bec the translocator recognize these 2 different start sites which to the transmem ptn with several helices within the mem 1
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Sat 7.11 Glycosylation of proteins at the endoplasmic reticulum (ER) Half of all eukaryotic proteins are glycosylated! The ER contains many proteins, - which are en ”in” route to other compartments. - Some proteins with a retention signal remain in the lumen of the ER and are responsible for correct folding of other proteins or catalyzing disulfide bonds in proteins ( protein disulfide isomerase ). In the ER transfer of glycosyl- groups on the proteins is usually found. Glycosylation is of major impact for medicine , since blood groups or aspects of immuno rejection after transplantation depends on the glycosylation of proteins. Most of the proteins are glycosylated in the rough ER at asparagine residues ( N -linked glycosylation ). Half of all eukaryotic proteins are glycosylated! The covalent bonding of sugars to proteins is a major task of the ER. About half of the eukaryotic proteins are glycosylated. Most of the ER proteins but - only few in the cytosol are glycosylated (using O-bonding to serine or threonine residues). 2
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- 90% of glycosylated proteins contain N-linked sugars.
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