Cell Biology Tutorial: Membrane Proteins
Note: This is a reference for educational/studying purposes, not a question, please save all comments or questions for the end.
\({\bf{Three~Types}}\) - integral/transmembrane proteins: span the membrane and contain hydrophilic cytosolic and exoplasmic domains + hydrophilic membrane-spanning domains - lipid-anchored membrane proteins: bound to lipid molecules, has tail embedded into the leaflet which anchors the protein to the membrane, does not span the bilayer - peripheral membrane proteins: bound indirectly through lipid anchor or integral proteins, can be associated with cytoskeletal elements or the ECM \({\bf{Membrane~Spanning~Structures}}\) typically alpha-helices w/ hydrophobic side chains pointing away from the heli and interacting with the bilayer while the carbonyl groups form hydrogen bonds with the amino acids on the C-terminus - can be single pass (Glycophorin A) or multipass (bacteriorhodopsin) - aquaporins: transport water, glycerol, and other hydrophilic molecules, may have alpha-helices that cross membrane halfway and/or at oblique angles - annular phospholipids: ring of lipids around protein - electrostatic interactions between positive and negatively charged amino acid side chains -> guide assembly of membrane proteins - porins: transmembrane proteins characterized by beta barrels where outer surface is hydrophobic and the core is hydrophilic. nonpolar b-strands form ring/band around the barrel
\({\bf{Anchoring~Proteins}}\) - lipids may anchor water-soluble proteins to one leaflet, protein itself does not enter bilayer - three groups: 1. fatty acyl group on N-terminal glycine residue (acylation) 2. hydrocarbon chain on cysteine residue on C-terminus (prenylation) 3. GPI anchors, contain phosphatidylinosol and phosphoethanolamine which anchors the membrane to the C-terminus of the protein - glycoproteins are oriented so that their carb. chains are in the exoplasmic domains \({\bf{Lipid~Binding~Motifs}}\) - peripheral proteins bind to the head groups of phospholipids - ring of positively charged arginine and lysine around catalytic channel - enzymatic calcium+ active sites become buried in the hydrophobic amino acid channel \({\bf{Detergents}}\) amphiphatic molecules that disrupt phospholipid bilayers - detergent concentration increases -> micelle formation - critical micelle formation: concentration at which micelles form, unique to each detergent - ionic detergents: bind to hydrophobic regions of membrane proteins/water-soluble proteins - non-ionic detergents: form mixed micelles that are not soluble - peripheral proteins can be removed with highly ionic solutions which disrupt bonds but most peripheral proteins are already soluble in water
This is the end of my tutorial; I hope you found it helpful. If you have any ∗relevant∗ comments or questions I will attempt to address them to the best of my ability. Thank you for reading!
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