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Glucose on the sugar side chains of proteins keeps unfolded proteins in the ER. Mannoses on sugar side chains act as a timer for protein folding. Unfolded proteins in the ER are threaded through a retrotranslocon into the cytosol where they are ubiquitylated and digested. IRE1, ATF6 and PERK sense the amount of unfolded protein and generates several responses to reduce the effects and amount of unfolded protein.
The secondary structure of a protein is generated by the way in which its amino acids interact through the intermolecular bond. These interactions create a spatial conformation of the polypeptide chain. The two most studied secondary conformations of proteins are the alpha-helix and the beta-sheet.ny changes in the structure of a protein are relevant if they alter its biological activity. Changes in the primary structure of a protein are the most important because they are modifications in the composition of the molecule, and that composition determines all the other structures of the protein.