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ACS BIOCHEMISTRY EXAM: – QUESTIONS/ANSWERS
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ACS BIOCHEMISTRY EXAM: – QUESTIONS/ANSWERS
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ACS BIOCHEMISTRY EXAM: – QUESTIONS/ANSWERSWhen glucose is totally oxidized to CO₂ and H₂O, how many ATP molecules are
made by oxidative phosphorylation relative to the maximum yield? Right
Ans - 26 out of 30
Substrate level phosphorylation Right Ans - ATP synthesis when the
phosphate donor is a substrate with high phosphoryl transfer potential
Function of thioester intermediate such as the one formed from GAP
dehydrogenase Right Ans - allows the two-step reaction to be coupled so
the second reaction (energetically unfavorable phosphorylation), can proceed
How many ATP or GTP equivalents are produced during one turn of the CAC?
Right Ans - 10
Why is the T state of glycogen phosphorylase less active? Right Ans - the
active site is partially blocked
Normal glucose concentration in blood Right Ans - 80-120 mg/100 mL
Why is glycogen branching important? Right Ans - increases glycogen
solubility and increases glycogen synthesis and degradation by increasing
potential sites of action
What regulates phosphorylase kinase? Right Ans - calcium ions, protein
kinase a
acid Right Ans - proton donor
base Right Ans - proton acceptor
pH Right Ans - -log[H⁺]
pOH Right Ans - -log[OH⁻]
pKa Right Ans - -logKa
,buffer Right Ans - resists changes in pH, composed of weak acid and its
conjugate base or a weak base and its conjugate acid
buffer range Right Ans - pH = pKa ± 1
maximum buffering capacity Right Ans - when [HA] = [A-] and hence when
pH = pKa, high concentrations of HA/A-
half equivalence point Right Ans - pH = pKa
equivalence point Right Ans - moles HA = moles NaOH
Henderson-Hasselbalch equation Right Ans - pH = pKa + log [A-]/[HA]
zwitterion Right Ans - A molecule that contains charges, but is neutral
overall. Most often used to describe amino acids
basic amino acids (positive charge) Right Ans - arginine, lysine, histidine
acidic amino acids (negative charge) Right Ans - aspartic acid, glutamic
acid
non polar amino acids Right Ans - Glycine, Alanine, Valine, Leucine,
Isoleucine, Methionine, Phenylalanine, Tryptophan, Proline
polar amino acids Right Ans - Serine, Threonine, Tyrosine, Asparagine,
Glutamine, Cysteine
amino acids with OH group Right Ans - serine, threonine, tyrosine
amino acids with sulfur Right Ans - cysteine and methionine
amino acid capable of making disulfide bonds Right Ans - cysteine
isoelectric point Right Ans - The pH value at which the amino acid exists as
a zwitterion
ionizable Right Ans - to convert wholly or partially into ions
, D amino acid Right Ans - amino group on the right
L amino acid Right Ans - amino group on the left, all amino acids found in
eukaryotes
primary structure Right Ans - sequence of amino acids, determines 3D
shape of peptide
secondary structure Right Ans - H bonding in the backbone, alpha-helix,
beta-sheet
alpha-helix Right Ans - the spiral shape resulting from the coiling of a
polypeptide in a protein's secondary structure, 3.6 residues per turn
beta-sheet Right Ans - planar pleat arrangement
parallel beta-sheet Right Ans - all bonded strands have the same N to C
direction, separated by long sequence distances, less stable
anti-parallel beta-sheet Right Ans - protein chains running in opposite
directions, more stable due to optimal H bonding
tertiary structure Right Ans - interactions between amino acid side chains,
3D folding of a single peptide
quaternary structure Right Ans - the interaction between peptides in
proteins that contain multiple subunits (i.e. hemoglobin)
cooperativity Right Ans - a form of allosteric regulation that can amplify
enzyme activity
globular proteins Right Ans - hydrophobic residues sequestered in the
interior of the protein, while hydrophilic residues are on the outer surface
membrane proteins Right Ans - embedded proteins that perform specific
functions for the cell membrane.
fibrous proteins Right Ans - long, insoluble, structural proteins
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