BIOLOGY 1A03 Lecture 6: Protein Folding and Leaving the Endomembrane System

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BIOLOGY 1A03 Full Course Notes
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BIOLOGY 1A03 Full Course Notes
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Recall that the amphipathic properties of the phospholipids was essential for the formation of the bilipid membrane. The hydrophilic head groups face the aqueous environment of the cytosol or the exterior of the cell and the hydrophobic core is hidden in the core of the membrane. In the same way, the side chains of the amino acid residues, whether they are hydrophilic or hydrophobic, determines the overall three-dimensional shape of the protein. Previously, we highlighted the important cellular functions that can be played by proteins, all proteins have distinct three- dimensional shapes that are critical to their functions. The three dimensional folded shape of that polypeptide is essential to allow for the proper function of the protein. All proteins, whether synthesized by free or bound ribosomes take on a three-dimensional folded shape. Here we see a globular protein found in the cytosol. The exterior of the protein is hydrophilic, allowing the protein to be soluble in the cytosol.

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