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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.
Alpha Helices. Alpha helices are the most common form of secondary structure in proteins. They are created by right-handed coiling of the primary protein structure. The coiling is caused by hydrogen bond interactions between the amino acids within the protein.Alpha helices are often found in DNA binding motifs.n the cytoplasm, ribosomes will interact with the transcript and create a protein (polypeptide) from individual amino acids. This process is called translation and produces the primary protein structure. Secondary protein structure is the general 3-dimensional form of local segments of a protein.