MBB 231 Lecture Notes - Lecture 7: Glycophorin, Cytosol, Arginine

• School: Simon Fraser University
• Department: Molec Biol & Biochem
• Course: MBB 231
• Professor: Ingrid Northwood

Document Summary

Several transmembrane polypeptide chains span the membrane in an a-helical conformation consisting of. 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. Some transmembrane proteins are arranged as b-sheets in the form a closed b-sheet conformation known as b-barrels: this structure is common in pore-forming transmembrane proteins called porins. Peripheral proteins: hydrophilic proteins that are located on the surface of the membrane where they are non- Covalently linked to the polar head groups or hydrophilic parts of other membrane proteins. These proteins will be released by change in ph, ionic strength of a buffer, or the addition of urea or carbonate.