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Chapter 17.4.2

Post-Translational Modifications

QuestionAnswer
protein folding during synthesis, polypeptide chain begins to coil/fold into 3-D molecule with secondary and tertiary structure -gene determines primary structure, which in turn determines shape
post-translational modification Changes to the new protein before it can perform final function -ex: phosphorylation or two or more polypeptide chains coming together to form quaternary structure of Hemoglobin
chaperoins protein molecules that assist the proper folding of other proteins
free ribosomes in the cytosol -mostly synthesis proteins that function in the cytosol -ribosomes are identical so can switch from free to bound and vice versa
bound ribosomes attached to outside of ER or nuclear envelope -proteins destined for endomembrane system or secreted from cell
location of polypeptide synthesis always begins in cytoplasm unless ribosome attached to the ER
signal peptide located on polypeptide chain -makes it so that ribosome knows the protein is destine for ER or secretion
signal recognition particle (SRP) protein the binds to signal peptide and brings it and its ribosome to the ER
Polyribosomes multiple ribosomes translating mRNA at the same time -enables cell to make many copies of particular polypeptide quickly
bacterial cells -coupling of transcription and translation -bacterial DNA isn't bound by nucleus, so new proteins can quickly diffuse to target site
Created by: maddiemiller
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