ACS BIOCHEMISTRY EXAM STUDY QUESTIONS AND ANSWERS WITH COMPLETE SOLUTIONS GRADED A 2024
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Course
ACS BIOCHEMISTRY
Institution
ACS BIOCHEMISTRY
Henderson-Hasselbach Equation - pH = pKa + log ([A-] / [HA])
FMOC Chemical Synthesis - Used in synthesis of a growing amino acid chain to a polystyrene bead. FMOC is used as a protecting group on the N-terminus.
Salting Out (Purification) - Changes soluble protein to solid precipitate. Protei...
ACS BIOCHEMISTRY EXAM STUDY
QUESTIONS AND ANSWERS WITH
COMPLETE SOLUTIONS GRADED A
2024
,
MUGWE [Date] [Course title]
,Henderson-Hasselbach Equation - pH Affinity Chromatography - Attach a
= pKa + log ([A-] / [HA]) ligand that binds a protein to a bead.
Elute with harsh chemicals or similar
ligand.
FMOC Chemical Synthesis - Used in
synthesis of a growing amino acid
chain to a polystyrene bead. FMOC is SDS-PAGE - Uses SDS. Gel is made
used as a protecting group on the N- from cross-linked polyacrylamide.
terminus. Separates based off of mass with
smaller molecules moving faster.
Visualized with Coomassie blue.
Salting Out (Purification) - Changes
soluble protein to solid precipitate.
Protein precipitates when the charges SDS - Sodium dodecyl sulfate.
on the protein match the charges in Unfolds proteins and gives them
the solution. uniform negative charge.
Size-Exclusion Chromatography - Isoelectric Focusing - Variation of gel
Separates sample based on size with electrophoresis where protein charge
smaller molecules eluting later. matters. Involves electrodes and pH
gradient. Protein stops at their pI
when neutral.
Ion-Exchange Chromatography -
Separates sample based on charge.
CM attracts +, DEAE attracts -. May FDNB (1-fluoro-2,3-dinitrobenzene) -
have repulsion effect on like charges. FDNB reacts with the N-terminus of
Salt or acid used to remove stuck the protein to produce a 2,4-
proteins. dinitrophenol derivative that labels
the first residue. Can repeat
hydrolysis to determine sequential
Hydrophobic/Reverse Phase amino acids.
Chromatography - Beads are coated
with a carbon chain. Hydrophobic
proteins stick better. Elute with non- DTT (dithiothreitol) - Reduces
H-bonding solvent (acetonitrile). disulfide bonds.
, Iodoacetate - Adds carboxymethyl Turns once every 3.6 residues.
group on free -SH groups. Blocks Distance between backbones is 5.4Å.
disulfide bonding.
Helix Dipole - Formed from added
Homologs - Shares 25% identity with dipole moments of all hydrogen bonds
another gene in an α-helix. N-terminus is δ+ and C-
terminus is δ-.
Orthologs - Similar genes in different
organisms ß-sheet - Either parallel or anti-
parallel. Often twisted to increase
strength.
Paralogs - Similar "paired" genes in
the same organism
Anti-parallel ß-sheet - Alternating
sheet directions (C & N-termini don't
Ramachandran Plot - Shows favorable line-up). Has straight H-bonds.
phi-psi angle combinations. 3 main
"wells" for α-helices, ß-sheets, and
left-handed α-helices. Parallel ß-sheet - Same sheet
directions (C & N-termini line up).
Has angled H-bonds.
Glycine Ramachandran Plot - Glycine
can adopt more angles. (H's for R-
group). ß-turns - Tight u-turns with specific
phi-psi angles. Must have gly at
position 3. Proline may also be at ß-
Proline Ramachandran Plot - Proline turn because it can have a cis-omega
adopts fewer angles. Amino group is angle.
incorporated into a ring.
Loops - Not highly structured. Not
α-helices - Ala is common, Gly & Pro necessary highly flexible, but can
are not very common. Side-chain occasionally move. Very variable in
interactions every 3 or 4 residues. sequence.
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