MBB 231 Lecture Notes - Lecture 7: Cytoplasm, Cysteine, Hydrolysis
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9 Dec 2015
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Integral proteins are embedded within the lipid bilayer and are held in place by the affinity of hydrophobic. Segments of the proteins for the hydrophobic interior of the lipid bilayer. The treatment with detergent, disrupts the lipid bilayer and is necessary to solubilize and extract integral. Integral proteins that are embedded in and protrude outward from only one side of the bilayer are known as integral. Transmembrane proteins span the membrane and have hydrophilic regions protruding from the membrane on both. Several transmembrane polypeptide chains span the membrane in an a-helical conformation consisting of. 20-30 amino acid residues with hydrophobic r groups. Terminus (outer): type 3: a single polypeptide that spans the membrane multiple times, type 4: multiple polypeptides that span the membrane. Example: glycophorin (type 1: a major protein exposed on the outer surface of human red blood cells and exists as a, contains positively charged arginine and lysine residues near the cytosolic face and deep anchors.
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