beta(1-4) N-acetyl-D-Glucosamine *add amine group to carbon 2-makes the molecule bigger-that changes H+ bonding making it slightly less hydrophobic
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Cisternal progression
no leaving, just hanging out until they're ready
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Clathrin
-forms flexible cages or protein called triskelions
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COPI
transports proteins between Golgi compartments
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COPII
transports proteins from ER to Golgi-chases escapees from the Golgi
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D
-OH on the right-OH in the up position
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Digestion of starch
amylase, alpha-glucosidase, and debranching enzyme
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Disaccharide
2 monosaccharides
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Endoglycosidases
cleaves middle of sugar chain at glycosidic bond
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Epimers
differ at exactly one chiral carbon
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Example of a glycosaminoglycan
hyaluronic acid, heparin
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example of sphingolipid
Sphingomyelin, ceramide
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exoglycosidases
cuts terminal sugar at glycosidic bond
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Extrinsic membrane proteins
-bind via electrostatic and H+ bonding-easy to remove-change pH
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fatty acid definition
carboxylic acid with a long chain hydrocarbon side group (tail)
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Fatty Acylated Lipid-Linked Proteins
Myristic acid and palmate acid
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Flippase
Catalyzes outer to inner leaflet flip of lipids
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fluid mosaic model
-membrane is not static-proteins can be imbedded
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fluidlike properties of a bilayer
-Layers are not static-transverse (flip-flopping) of lipids-lateral diffusion-constant rotation around c-c bonds of lipid tails-temperature dependant
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Fluorescence Recovery After Photobleaching (FRAP)
A method used to study the movement of proteins within living cells.
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function of glycoforms
1) define protein structures2) mediated recognition events3) antigenic Determinants
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gangliosides
ceramide linked to an oligosaccharide
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Glucocorticoids
affect carbohydrate, protein and lipid metabolism
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glycoforms
same protein with variation in sequence, location, and number of covalently attached carbohydrates
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Glycosaminoglycans structure
alternating uronic and hexoamine residue-unbranched
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glycosidic bond
Anomeric carbon condenses with alcohol-alpha-beta
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glycosylated
proteins with oligosaccharide covalantly attached
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GPI-linked proteins
located only on the exterior surface of the plasma membrane
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Heteropolysaccharides
different monosaccharides
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Homopolysaccharides
same monosaccharides
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how are cyclic sugars made?
By the alcohol on the last carbon chiral carbon reacting with the carbonyl group
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How are membrane lipids distributed?
asymmetrically
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how are new membranes formed?
created by expanding existing membranes
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how are proteins directed?
-carbohydrate recognition-C-terminal sequences
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how are the the oligosaccharides attached to proteins?
N linked then Asn-X-Ser or Thr*X can be any amino acid except Pro and rarely Asp-then it is chopped until there is only 3 mannoses making the Y-other molecules can be added to the mannoses after the chopping
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how do coated vesicles preserve orientation?
-inside of the membrane is the same as the ER and Golgi and outside of the cell-stays in the same environment
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how do membrane lipids get to the outer leaflet
its flops out
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how do the polar heads sit in the bilayer?
they nestle in right next to each other
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How do we end up with trans fat?
-to preserve shelf life and avoid oxidation of unsaturated fats, the unsaturated fats are hydrogenated to reduce some double bounds-this converts the cis bonds to trans
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how do you know which carbon has a double bond?
Delta symbol C# that starts the double bond
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how do you number the rings?
clockwise from the anomeric carbon
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How does cholesterol affect membrane fluidity?
decreases fluidity
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how does glycogen debranching enzyme work?
breaks the alpha(1-6) bond
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How does glycogen phosphorylase work?
breaks the Alpha(1-4) from the nonreducing ends
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how does temperature effect the bilayer?
-above transition temperature - liquid crystal (liquid but organized- below - gel like solid
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How many monosaccharides are in a polysaccharide?
3 or more
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how to biological membrane fuse?
by proteins called SNAREs
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How to name glycosidic bonds?
Greek letter ( C# mononsaccharide 1 - C# monosaccharide 2)
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how to name monosaccharides
-functional group-carbon number-stereochemistry of last chiral carbon
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How to name triacylglycerols?
by adding -oyl to the end of each fatty acid and ending with glycerol
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how to remove extrinsic membrane proteins?
-add salt-interupt bonding using Urea
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how to translocons work?
-transmembrane proteins enter the channel- alpha helix opens to lipid bilayer releasing into lipid bilayer
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inner leaflet
The layer of the cell membrane phospholipid bilayer that faces the cytoplasm.
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integral proteins
penetrate the hydrophobic interior of the lipid bilayer
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Ketone functional group and suffix
ketose
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L
-OH on the left-OH in the down postion
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lateral diffusion
movement within the same plane
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Lipid bilayer formation
-driven by hydrophobic effect-size constraints
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Lipid definition
non-polar organic molecule
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lipid linked proteins
-lipid acts as on anchor in the bilayer
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Liposome
closed self sealing solvent filled vesicles bound by a single bilayer
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membrane fusion
1) zipping SNARES2) Hemifusion: Exposes the bilayer interior3) Fusion Pore: tension from SNAREs causes breakdown of the original bilayer forming new ones
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Mineralocorticoids
regulate salt and water balance
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Monosccharides composition
Aldehyde or ketone, 3+ carbons, polyhydroxy alcohols
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Mutarotation
switching between D and L
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Myristic Acid
-C14, saturated-aminde linkage, Thioester-myristoylation stable for life-located cytosol, endoplasmic reticulum, inner face of plasma membrane and nucleus
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O-linked oligosaccharides
*have glycosidic bond to the hydroxyl group of Ser or Thr residues*synthesized in the Golgi*more common*condensation Rxn