BLG 311 Lecture Notes - Lecture 2: Membrane Transport Protein, Lipid Bilayer, Membrane Transport
24 May 2016
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Document Summary
The covalent addition of oligosaccharides (sugar groups) to proteins (on the extracellular face) Special amino acids are glycosylated on: serine, asparagine. They aid in folding, identity and adhering to other extracellular matrix and other cells. Cysteine amino acid residues react to each other to form sulphur to sulphur bridges. Extracellular matrix is where they occur because the cytosol is a reducing environment where the bridge cannot form (need oxidizing environment) The ss bridge is helped to be formed by the er (more likely here) and peroxisomes. Most transmembrane proteins cross the membrane as a hydrophobic alpha-helix. Hydrophobicity can be measured in a hydropathy plot. Take sections of the protein and score based on non-polar characteristics (positive values for non- polar) The peaks that are hydrophobic can explain the domains that pass through the membrane (so the number of peaks that"s how many times they pass through the membrane) Dividing the membrane: the sperm cell has three plasma membrane.
