BIOSC-116 Lecture Notes - Lecture 27: Integral Membrane Protein, Facilitated Diffusion, Hydrophile
9 Oct 2020
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Document Summary
Many substances can"t go through the membrane and proteins provide a hydrophilic path that allows them to go through by the protein changing shape and pushing the substance through. Some proteins are enzymes for ex in etc. The proteins on the outside membrane bind with hormone and they trigger changes on the inside membranes and through transduction a signal goes through the cell. Proteins on the inside and outer membrane of the lipid bilayer can be used for attachment such as cytoskeleton and cell to cell recognition. Most integral proteins go through the bilayer and interact with both aqueous environments around the bilayer. Hydrophobic core contains regions that have nonpolar amino acids (area that is inside the membrane with the hydrophobic lipids) These hydrophobic chains consist of about 17-20 amino acids. The integral proteins are linked together by portions of a protein (polar amino acids since its outside) They are connected by non-covalent bonds- hydrogen and ionic bonds.
