| Question |
Answer |
| 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 |
HHS Shrek
