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ACS BIOCHEMISTRY EXAM QUESTION WITH COMPLETE SOLUTIONS LATEST 2023/2024
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ACS BIOCHEMISTRY EXAM QUESTION WITH COMPLETE SOLUTIONS LATEST 2023/2024 ACS BIOCHEMISTRY EXAM QUESTION WITH COMPLETE SOLUTIONS LATEST 2023/2024 ACS BIOCHEMISTRY EXAM QUESTION WITH COMPLETE SOLUTIONS LATEST 2023/2024

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  • December 18, 2023
  • 34
  • 2023/2024
  • Exam (elaborations)
  • Questions & answers

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  • acs biochemistry exam
  • acs
  • biochemistry
  • acs biochemistry exam question with complete solu

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ACS BIOCHEMISTRY EXAM QUESTION WITH
COMPLETE SOLUTIONS LATEST 2023/2024

Henderson-Hasselbach Equation - ANSWER--pH = pKa + log ([A-] / [HA])


FMOC Chemical Synthesis - ANSWER--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) - ANSWER--Changes soluble protein to solid precipitate.
Protein precipitates when the charges on the protein match the charges in the
solution.


Size-Exclusion Chromatography - ANSWER--Separates sample based on size with
smaller molecules eluting later.


Ion-Exchange Chromatography - ANSWER--Separates sample based on charge.
CM attracts +, DEAE attracts -. May have repulsion effect on like charges. Salt or
acid used to remove stuck proteins.


Hydrophobic/Reverse Phase Chromatography - ANSWER--Beads are coated with a
carbon chain. Hydrophobic proteins stick better. Elute with non-H-bonding
solvent (acetonitrile).


Affinity Chromatography - ANSWER--Attach a ligand that binds a protein to a
bead. Elute with harsh chemicals or similar ligand.

, ACS BIOCHEMISTRY EXAM QUESTION WITH
COMPLETE SOLUTIONS LATEST 2023/2024

SDS-PAGE - ANSWER--Uses SDS. Gel is made from cross-linked polyacrylamide.
Separates based off of mass with smaller molecules moving faster. Visualized with
Coomassie blue.


SDS - ANSWER--Sodium dodecyl sulfate. Unfolds proteins and gives them uniform
negative charge.


Isoelectric Focusing - ANSWER--Variation of gel electrophoresis where protein
charge matters. Involves electrodes and pH gradient. Protein stops at their pI
when neutral.


FDNB (1-fluoro-2,3-dinitrobenzene) - ANSWER--FDNB reacts with the N-terminus
of the protein to produce a 2,4-dinitrophenol derivative that labels the first
residue. Can repeat hydrolysis to determine sequential amino acids.


DTT (dithiothreitol) - ANSWER--Reduces disulfide bonds.


Iodoacetate - ANSWER--Adds carboxymethyl group on free -SH groups. Blocks
disulfide bonding.


Homologs - ANSWER--Shares 25% identity with another gene


Orthologs - ANSWER--Similar genes in different organisms


Paralogs - ANSWER--Similar "paired" genes in the same organism

, ACS BIOCHEMISTRY EXAM QUESTION WITH
COMPLETE SOLUTIONS LATEST 2023/2024


Ramachandran Plot - ANSWER--Shows favorable phi-psi angle combinations. 3
main "wells" for α-helices, ß-sheets, and left-handed α-helices.


Glycine Ramachandran Plot - ANSWER--Glycine can adopt more angles. (H's for R-
group).


Proline Ramachandran Plot - ANSWER--Proline adopts fewer angles. Amino group
is incorporated into a ring.


α-helices - ANSWER--Ala is common, Gly & Pro are not very common. Side-chain
interactions every 3 or 4 residues. Turns once every 3.6 residues. Distance
between backbones is 5.4Å.


Helix Dipole - ANSWER--Formed from added dipole moments of all hydrogen
bonds in an α-helix. N-terminus is δ+ and C-terminus is δ-.


ß-sheet - ANSWER--Either parallel or anti-parallel. Often twisted to increase
strength.


Anti-parallel ß-sheet - ANSWER--Alternating sheet directions (C & N-termini don't
line-up). Has straight H-bonds.


Parallel ß-sheet - ANSWER--Same sheet directions (C & N-termini line up). Has
angled H-bonds.

, ACS BIOCHEMISTRY EXAM QUESTION WITH
COMPLETE SOLUTIONS LATEST 2023/2024


ß-turns - ANSWER--Tight u-turns with specific phi-psi angles. Must have gly at
position 3. Proline may also be at ß-turn because it can have a cis-omega angle.


Loops - ANSWER--Not highly structured. Not necessary highly flexible, but can
occasionally move. Very variable in sequence.


Circular Dichroism - ANSWER--Uses UV light to measure 2° structure. Can be used
to measure destabilization.


Disulfide-bonds - ANSWER--Bonds between two -SH groups that form between 2°
and 3° structure.


ß-mercaptoethanol - ANSWER--Breaks disulfide bonds.


α-keratin - ANSWER--formed from 2 α-helices twisted around each other. "Coiled
coil". Cross-linked by disulfide bonds.


Collagen - ANSWER--Repeating sequence of Gly-X-Pro. 3 stranded "coiled coil".
Contains gly core.


Myoglobin 4° Structure - ANSWER--Symmetric homodimer,


Hemoglobin 4° Structure - ANSWER--Tetramer. Dimer of dimers. α2ß2 tetramer.

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