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42 Cards in this Set
- Front
- Back
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4 classes of large biological molecules
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nucleic acids
lipids (fats) proteins carbohydrates |
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dehydration reaction or synthesis
(polymer formation) |
two monomers covalently bond to each other, losing a water molecule
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hydrolysis
(polymer disassembly) |
the bond between monomers is broken due to the addition of a water molecule
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monosaccharides
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simple sugars
multiples of CH2O glucose (C6H12O6) is the most common |
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disaccharides
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two sugars
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polysaccharides
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many sugars
long polymers of sugar cellulose = glucose + beta glycosidic linkages starch = glucose + alpha glycosidic linkages glycogen = glucose + alpha glycosidic linkages |
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glucose
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preferred source of energy for many organisms
attracts and holds water |
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glycogenesis
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dehydration synthesis
catalyzed by an enzyme called glycogen synthase |
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glycogenloysis
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glycogen is broken down into glucose for use by the body
catalyzed by an enzyme called glycogen phosphorylase |
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enzyme regulation
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regulated by phosphorylation
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phosphorylation
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covalent addition of phosphate to an enzyme via dehyrdation synthesis
can either turn an enzyme "on" (increase its catalytic rate) or turn it "off" (decrease its rate) |
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what can proteins do
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storage
defensive hormonal structural transport receptor enzymatic muscle contraction (actin and myosin) |
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what are the 4 levels of protein structure
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primary
secondary tertiary quarternary |
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primary structure of a protein
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sequence of amino acids
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secondary and tertiary structures
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interactions between amino acids form formal structure
**bonding and folding |
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quaternary structure
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multiple subunits
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substrate
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molecule that is going to be changed by the enzyme
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catalytic cycle of an enzyme
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1. substrates enter active site
2. substrates are held in active site by weak interactions 3. active site can lower Ea (activation energy) and speed up a reaction 4. substrates are converted to products |
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activation energy
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amount of energy to go from a substrate to product
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regulation of enzyme activity
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temperature
pH co-factors (non-organic molecules) co-enzymes (organic molecules) inhibitors affinity for the substrate |
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enzyme inhibition
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reduction of the production of an enzyme
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competitive enzyme inhibition
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both the substrate and the inhibitor are competing for the active site
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noncompetitive enzyme inhibitor
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inhibitor acting away from the active site
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cell membrane structure
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phospholipid bilayer
hydrophilic on both sides hydrophobic in the middle regulates entry/exit |
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integral protein
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enter hydrophobic interior of the membrane
nonpolar amino acids in hydrophobic region of protein hydrophilic region of protein on either (aqueous) side hydrophilic channel in center of some proteins |
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peripheral protein
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not embedded in lipid bilayer at all
loosely bound to surface |
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cell membrane - fluidity
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membranes not static
weak hydrophobic interactions molecules move laterally cholesterol (steroid, lipid) = fluidity buffer |
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cell membrane - mosaic
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not homogenous
-each type of cell has different proteins -the types of proteins present determine the function of the membrane for that cell |
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membrane protein functions
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transport
enzymatic activity signal transduction cell-cell recognition intracellular joining attachment to the cytoskeleton and extracellular matrix |
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g-protein
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sends a signal
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diffusion
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passive transport
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ion channels
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transmembrane proteins
"gated" to control ion movement gates respond to a stimulus (electrical signal, ligand binding, stretch) |
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prokaryotic vs eukaryotic cells
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size difference
nucleus v. nucleoid cell membrane cell organelles flagella cilia |
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cell wall (only plants)
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cellulose, for structure
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cell (plasma) membrane
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semipermeable barrier
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chondroplast (only plants)
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photosynthesis
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endoplasmic reticulum (rough and smooth)
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sacs and tubes (surfaces for synthesis and metabolism)
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golgi apparatus
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synthesis, modification, sorting, and secretion of cellular products (protein folding)
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lysosome
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contains digestive enzymes
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mitochondrion
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cellular respiration (ATP production)
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nucleus
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contains chromatin (DNA)
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Ribosome
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protein synthesis
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