Membrane Cheat Sheet
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This 3 page Bundle was uploaded by Luke Holden on Sunday August 28, 2016. The Bundle belongs to BIOL 4610 at Clemson University taught by Susan Chapman in Fall 2016. Since its upload, it has received 17 views.
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Date Created: 08/28/16
Membrane lipids LIPID STRUCTURE BASE IDENTIFIERS Phospholipid Polar head group Glycerol (fatty Amphipathic and fatty acid/acyl acid tail at Most abundant Phosphate oxygen 1 & 2) Kind and backbone Sphingosine proportions vary 3 oxygens (fatty acid tail among at oxygen 2) membranes Glycolipid Sugar head Glycerol Form by the Sphingosine addition of carbohydrates to lipids Most common are cerebrosides (uncharged sugar as head group) Prominent in brain and nerve cells Most located in the outer membrane layer of animal cells amphipathic Sterol 4 rigid & planar, Eukaryotic fused ring membranes structure contain significant Hydroxyl group amount attached to ring Animals structure to help cholesterol orient within o Fluidity membrane and buffer bond to polar Plantphytosterols head Fungalergosterol amphipathic The movement of lipids from one monolayer to another (transverse diffusion) is rare o Occur when phospholipid translocators or flippases are present Membrane fluidity changes with temperature (Tm transition temperature) Lipids move within their monolayer o Rotation o Lateral diffusion Membrane Proteins PROTEIN WHERE IDENTIFIERS EXAMPLES Integral Embedded in Difficult to Transmembrane Protein Membrane the lipid remove/isolate Cross once (singlepass Proteins bilayer b/c of from membrane proteins) hydrophobic Integral Cross several times region monotropic (multipass proteins) proteins are Anchored to the lipid bilayer embedded in one by one or more hydrophobic layer transmembrane segments Transmembrane Example: B barrel proteins span the Singlepass Membrane Protein membrane and C & Nterminus on either end protrude on both of the membrane sides Glycophorin Detergents pull Multipass Membrane Protein apart the 220 transmembrane membrane and segments surround the bacteriohodopsin protein o Micelles prevent the protein from breaking down Peripheral Hydrophilic Easy to remove regulatory protein subunits of many Proteins and located from the ion channels and transmembrane on the membrane receptors surface of the Mostly bilayer, hydrophilic but attached some loosely to the hydrophobic head regions anchor them to the membrane Electrostatic forces and hydrogen bonding (weak) Easy to isolate by altering pH or ionic strength Chelating agents are used to solubilize them Lipid Hydrophilic Reside on Fatty acidanchored membrane Anchored and attached membrane protein Proteins to the bilayer surface Attached to a saturated fatty by covalent Linked to fatty acid, usually myristic (14C) or attachments acids (isoprenyl palmitic acid (16C) to lipid groups) Isoprenylated membrane proteins molecules Synthesized in the cytosol & that are modified by addition of embedded in multiple isoprenyl groups the bilayer (5C) usually farnesy (15C) or geranylgeranyl (20C) groups GPIanchored membrane proteins Covalently linked to gylcosylphosphatidylinositol Detergents are used to disrupt hydrophobic interactions and dissolve the lipid bilayer Proteins can be solubilized and extracted from membranes so that they can be studied o Ionic Detergents Sodium deoxycholate Sodium dodecylsulfate (SDS) Attach/bind around protein Break hydrogen bonds and straighten the protein out o Nonionic Detergents Triton X100 Octylglucoside Hello!
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