Section 1 Bio
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| Nonpolar Amino Acids | PGVIPMALT proline, glycine, valine, isoleucine, phenylalalanine, methionine, leucine, tryptophan
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| Positive Feedback | a downstream product returns to activate an earlier enzyme (occurs less often than negative feedback)
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| Secondary Structure | *patterns of hydrogen bonds bewteen backbone amide (H) and carboxyl (O) groups
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| Alpha Helix | *usu right handed helix that twists clockwise & makes a complete turn every 3.6 AA
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| Polar Amino Acids | CTTAGS cysteine, threonine, tyrosine, asparagine, glutamine, serine
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| Denaturing Agents and Forces Disrupted | *urea - hydrogen bonds
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| Acidic Amino Acids | *glutamic acid (glutamate)
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| Denaturation | *when protein conformation is disrupted & protein loses most 2º, 3º, 4º structure, not 1º bc covalent bonds
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| Quaternary Structure | *formed when 2 or more polypeptide chains bind together, each referred to as a subunit
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| Movement of Products of Glycolysis to the Matrix | *outer mito mem: permeable to sm molecules & both pyruvate & NADH pass via facilitated diffusion through porin, a lg membrane protein
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| Residue | each amino acid in a polypeptide chain
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| Amylospectin | form of starch that resembles glycogen but has a different branching structure
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| Fatty Acids | *long chains of carbons (usu even #, 24 max in humans) truncated at one end by a carboxylic acid
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| Glycoproteins | proteins that have carbohydrate groups attached that are a component of cellular plasma membrane
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| Glycolipid | *amphipathic lipids with one or more carbs attached
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| Kreb's Cycle (Citric Acid Cycle) | *each turn produces: 1 ATP (via substrate level phosphorylation), 3 NADH, 1 FADH2
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| Hydrogen Bond | *intermolecular force that allows H2O to maintain a liquid state in cellular environment (most cpds as light as H2O would be gas at high body temp, 37ºC/98.6ºF
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| How do most cell absorb glucose? | facilitated diffusion
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| Steroids | *4-ringed lipids
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| Liver and Glucose | the liver regulates the blood glucose level so liver cells are one of few cell types capable of reforming glucose form glycogen and releasing it back into the bloodstream
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| Negative Feedback | *when a product downstream in a reaction series comes back and inhibits enzymatic activity in an earlier reaction
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| Substrate Level Phosphorylation | formation of ATP from ADP & inorganic phosphate using the energy form the decay of high energy phosphorylated compounds as opposed to the energy from diffusion
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| Positive Cooperativity | the first substrate to bind changes the shape of the enzyme allowing other substrates to bind more easily
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| Amylose | form of starch that is an isomer of cellulose and may be branched or unbranched and has the same alpha-linkages as glycogen
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| Zymogen | *proenzyme
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| Steps of the CAC | OXALOACETATE (+acetyl CoA) → CITRATE → ISOCITRATE → (CO2, NAD+→NADH) α-KETOGLUTARATE → (CO2, NAD+→NADH) SUCCINYL CoA → (GDP→GTP) SUCCINATE → (FAD → FADH2) FUMARATE → MALATE → (NAD+→NADH) *repeat
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| Irreversible Inhibitor | bind covalently (a few noncovalently) to enzymes and disrupt their function, tending to be highly toxic
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| Nucleic Acid | polymer of nucleotides joined by phosphodiester bonds between the phosphate group of one nucleotide and the 3rd carbon of the pentose in the other nucleotide (DNA, RNA)
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| Acetyl CoA | *coenzyme
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| Reaction Rate and pH | enzymes function within specific pH ranges and denature when the pH is too far from the optimal pH (graph is like a normal curve)
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| Michaelis Constant (Km) | *the substrate concentration at which the reaction rate is equal to 1/2 Vmax
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| Starch | *carbohydrate polymer for storage in plants
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| Phosphatase | an enzyme which dephosphorylates something
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| Saturation Kinetics | *as relative concentration of substrate increases, the rate of rx also increases, but to a lesser and lesser degree until a max rate (Vmax) is reached
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| Prosthetic Groups | coenzyme that remains covalently bound to the enzyme throughout the reaction and emerges unchanged (e.g. heme)
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| Globular Tubulin | polymerizes under the right conditions to become a structure protein and makes up microtubules, the component of eukaryotic flagella and cilia
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| Primary Structure | number and sequence of amino acids, including the locations of disulfide bonds between cysteines
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