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ACS BIOCHEMISTRY CERTIFICATION SCRIPT 2026
QUESTIONS WITH SOLUTIONS GRADED A+
l kilo (k). Answer: 10^
l deci (d). Answer: 10^-
l centi (c). Answer: 10^-
l milli (m). Answer: 10^-
l micro (u). Answer: 10^-
l nano (n). Answer: 10^-
l pico (p). Answer: 10^-
l Eukaryotic cell characteristics. Answer: 5-100 micometers, some DNA contain histone, chromosomes in nuceus with membrane, mitosis, contain mitochondria, ER, golgi, lysosomes (animals), chloroplasts, absorpotion/ingestion/photosynthesis, unified pattern of metabolism/oxidative enzymes in mitochondria, contains cytoskeleton, exhibits intracellular movement
l Prokaryotic cell characteristics. Answer: 1-10 micrometers, DNA with nonhistone in nucleiod with NO membrane, fission/budding, no organelles/cytoskeleton/intracellular movement, absorption some photosynthesis, variation in metabolic patterns/oxidative enzymes on plasma membrane
l non polar amino acids. Answer: Glycine, alanine, proline, valine, leucine, isoleucine, methinonine (GAP V LIM)
l Aromatic R groups. Answer: Phenylalanine, Tyrosine, Tryptophan (FYW)
l Positively charged R groups. Answer: Lysine, arginine, histidine (KRH)
l Negatively charged R groups. Answer: Aspartate, glutamate (D, E)
l Polar, uncharged R groups. Answer: Serine, threonine, cysteine, asparagine, glutamine (STNCQ)
l Properties of peptide bonds. Answer: Planar due to double bond character in resonance structure, dipole moment due to electrophilic nature of the carbonyl carbon, transconfiguration of R groups due ot steric restrictions
l Roles of extra cellcular matrix. Answer: Cells organized into tissues and organs by adhesive interactions with extracellular matrix (also cell-cell adhesions). It provides a scaffold for. Formation of mineralized tissues (teeth and bones)
l 3 functions of cytoskeleton. Answer: Structure/organization to cytoplasm, determines cell shape, provides "tracks" for movement of vesicles and organelles
l 3 things that make up cytoskeleton. Answer: Microtubules, myofilaments, intermediate filament
l Role of trace elements 1% in cells. Answer: Bound by proteins and play key roles in catalytic or other activities
l Why is it that 99% of cell made with hydro, oxygen, nitrogen, and carbon?. Answer: Cell is mainly water (H2O), proteins (C, N, O, and H), nucleic acids, polysaccharides, lipids, macromolecular precursors, and metabolic intermediates made of all of these
l Difference between symmetric and asymmetric tetrahedral carbon atoms?. Answer: Symmetric bonds with at least 2 of the same atoms, aymmetric has 4 different atoms that its bonded to. It is considered a chiral carbon in this case.
l Monomer of protein. Answer: Amino acids
l Monomer of nucleic acids. Answer: Nucleotides
l Monomer of carbs- Polysaccharides. Answer: Simple sugars
l Monomer of lipids. Answer: fatty acids and glycerol
l Central dogma of DNA. Answer: DNA copies itself in replication, then DNA can be copied to RNA through trascription. Reverse transcription can happen as well. then RNA can be made into protein by translation. There is no flow of genetic info from protein to RNA or DNA.
l When glucose is oxidized (passing electrons to atmospheric oxygen to form water and CO2) what happens to entropy?. Answer: Entropy increase by the generation of 12 molecules of end products from each molecules of glucose plus 6 molecules of oxygen
l Draw Schematic of IgG. Answer: Draw it
l the midpoint of titration point is. Answer: inflection point.when pH and pKa are equal, and the amount of product/reactant are equal (acid=base)
l barcarbonate as buffer in blood. Answer: as more H+ ion accumulate in blood, bicarbonate is drive to combine with them to make carbonic acid, which then lets off water, and you get CO2 in the blood which converts to CO2 in the lungs.
l amount of dissolved CO2 in blood (water) is ______(high or low). Answer: low, bc CO2 is non polar, and it is unfavorable for it to stay in blood. another reason why bicarbonate rxn is driven down.
l what amino acid is the exception and does not have a chiral carbon?. Answer: glycine
l how do peptide bonds play a role in forming a protein. Answer: amino acids are linked by peptide bonds, and a protein consists of many amino acids
l polypeptide sequence always written with ___ on left and ___ on right. Answer: amino, C terminal
l primary structure of protein. Answer: sequence of AAs from amino terminal to carboxyl terminal
l secondary structure of protein. Answer: alpha helix, beta sheet, beta turn. 2ndary is sequence dependent, forms spontaneously, and stabilized hydrogen bonding
l alpha helix bonding. Answer: forms by hydrogen bonding between carbonyl oxygen and n+4 amino hydrogen.
l what affects alpha helix formation. Answer: interactions between R groups (3 or 4 residues apart), bulkiness of R group, occurrence of pro (ring) and gly. interactions between AA at ends of helical segment and electric dipole
l beta sheet formation. Answer: hydrogen bonding between adjacent strands, parallel/antiparallel
l beta turn formation. Answer: 180 degree turn in backbone, hydrogen bonding between 1st and 4th residue, most often with proline or glycine
l tertiary structure. Answer: B-a-B loop, B barrel. salt bridges help stabalize. ionic interactions between + and - AA side chains
l quaternary structure. Answer: two or more polypeptide chains. can be dimer, trimer, tetramer
l disulfide bonds are formed from the AA ___. Answer: cysteine. usually only occurs in proteins outside of cell (intracellular is reducing).
l myoglobin structure. Answer: single chain protein
l hemoglobin structure. Answer: four chain (tetramer) protein. dimer of AB dimers.
l allostery. Answer: binding of ligand to one site affects binding of ligands at another site. conformation changes in protein. it is what makes oxygen bind/saturate quickly in lungs
l MWC model. Answer: conerted model: all subunits undergo conversion simultaneously between low and high affinity forms
l the ligand that binds an antibody. Answer: antigen
l hemoglobin exhibits cooperative binding of its ligand meaning. Answer: it has a transition from a low affinity T state to high affinity R state
l immunoglobulins bind proteins. Answer: thru complimentarity w/n their variable domain
l covalent bond. Answer: atoms in a molecule share electrons
l ionic bond. Answer: polar part of a molecule hogs the electrons, forms a tight bond
l hydrogen bond. Answer: hydrogen acts as partial positive. it is bound to O, N, F
l AA with N, O will participate in. Answer: hydrogen bonding
l AA with no charge or a ring will participate in. Answer: vanderwaals
l charged AA will participate in. Answer: dipole-dipole (ionic)
l how does ligand bind to protein?. Answer: interactions with amino acid R groups that line binding site
l lower kd corresponds to ___ affinity of ligand for protein. Answer: higher
l one antibody can bind. Answer: 2 antigens
l enzyme reactions. Answer: are specific, lower free energy of activation, reduce time to reach equilibrium DO NOT change equilibrium constant (Keq) DO NOT change eq. [ ] DO NOT change free energy change for run (delta G)
l enzymes. Answer: biological catalysts accelerate metabolic rxns
l chymotrypsin mechanism. Answer: cleaves peptide bond between bulky hydrophobic AA (phe, trp, tyr, met)
l catalytic triad. Answer: serine, histidine, aspartate
l Michaelis-Menten equation. Answer: relates rate of enzymatic reactions to the reaction rate and the concentration of substrate.
l rate is dependent on. Answer: [substrate], [enzyme] (direct relationships), ph, temp (will have optimal for these 2)
l vmax. Answer: maximal rate. occurs at high [s], when enzyme is saturated. the bigger the vmax, the more powerful the enzyme
l kcat. Answer: vmax/[enzyme] at certain time.
l km. Answer: substate concentration when 1/2 vmax is reached. related to affenity of enzyme for substrate. lower km means stronger affinity for substrate.
l what does michaelis-menten plot look like?. Answer: hyperbolic curve (vo vs. [s])
