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Biology One

Section 1 Bio

QuestionAnswer
Nonpolar Amino Acids PGVIPMALT proline, glycine, valine, isoleucine, phenylalalanine, methionine, leucine, tryptophan
Positive Feedback a downstream product returns to activate an earlier enzyme (occurs less often than negative feedback)
Secondary Structure *patterns of hydrogen bonds bewteen backbone amide (H) and carboxyl (O) groups
Alpha Helix *usu right handed helix that twists clockwise & makes a complete turn every 3.6 AA
Polar Amino Acids CTTAGS cysteine, threonine, tyrosine, asparagine, glutamine, serine
Denaturing Agents and Forces Disrupted *urea - hydrogen bonds
Acidic Amino Acids *glutamic acid (glutamate)
Denaturation *when protein conformation is disrupted & protein loses most 2º, 3º, 4º structure, not 1º bc covalent bonds
Quaternary Structure *formed when 2 or more polypeptide chains bind together, each referred to as a subunit
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
Residue each amino acid in a polypeptide chain
Amylospectin form of starch that resembles glycogen but has a different branching structure
Fatty Acids *long chains of carbons (usu even #, 24 max in humans) truncated at one end by a carboxylic acid
Glycoproteins proteins that have carbohydrate groups attached that are a component of cellular plasma membrane
Glycolipid *amphipathic lipids with one or more carbs attached
Kreb's Cycle (Citric Acid Cycle) *each turn produces: 1 ATP (via substrate level phosphorylation), 3 NADH, 1 FADH2
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
How do most cell absorb glucose? facilitated diffusion
Steroids *4-ringed lipids
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
Negative Feedback *when a product downstream in a reaction series comes back and inhibits enzymatic activity in an earlier reaction
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
Positive Cooperativity the first substrate to bind changes the shape of the enzyme allowing other substrates to bind more easily
Amylose form of starch that is an isomer of cellulose and may be branched or unbranched and has the same alpha-linkages as glycogen
Zymogen *proenzyme
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
Irreversible Inhibitor bind covalently (a few noncovalently) to enzymes and disrupt their function, tending to be highly toxic
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)
Acetyl CoA *coenzyme
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)
Michaelis Constant (Km) *the substrate concentration at which the reaction rate is equal to 1/2 Vmax
Starch *carbohydrate polymer for storage in plants
Phosphatase an enzyme which dephosphorylates something
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
Prosthetic Groups coenzyme that remains covalently bound to the enzyme throughout the reaction and emerges unchanged (e.g. heme)
Globular Tubulin polymerizes under the right conditions to become a structure protein and makes up microtubules, the component of eukaryotic flagella and cilia
Primary Structure number and sequence of amino acids, including the locations of disulfide bonds between cysteines
Created by: rstones