BIOLOGY 2B03 Lecture Notes - Lecture 5: Immunoglobulin Light Chain, Sec61, Conformational Change

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Dynamic movements of the rer: the membranes of the er are constantly changing shape and structure, undergoing fission and fusion, and migrating to new locations in the cell. Protein glycosylation: n-linked: protein glycosylation is the addition of a polysaccharide or sugar group, to a protein, common on proteins that are secreted from the cell and the proteins embedded in the cell membrane. Important for proteins that mediate cell interactions with the extracellular matrix and for receptor-ligand recognition. Protein folding in the er: er is home to a collection of enzymes that facilitate protein folding. Disulphide bond formation in the er: covalent linkages between the sulfhydral groups (-sh groups) of two cysteine residues. Disulphide bonds in rnase a: pancreatic ribonuclease a (rnaase a) contains four disulphide bridges. Ire1 that is not associated with the bip will form homodimers in the er membrane: dimers are activated endonucleases.

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