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ACEDS/ACTUAL EXAM LATEST VERSION WITH VERIFIED QUESTIONS AND ANSWERS GRADED A+

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ACEDS/ACTUAL EXAM LATEST VERSION WITH VERIFIED QUESTIONS AND ANSWERS GRADED A+ Henderson-Hasselbach Equation - ANS--pH = pKa + log ([A-] / [HA]) FMOC Chemical Synthesis - ANS--Used in synthesis of a growing amino acid chain to a polystyrene bead. FMOC is used as a protecting group on the N-te...

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  • August 14, 2024
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  • 2024/2025
  • Exam (elaborations)
  • Questions & answers
  • ACEDS/ACTUAL
  • ACEDS/ACTUAL
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ACEDS/ACTUAL EXAM LATEST
VERSION 2024-2025 WITH VERIFIED
QUESTIONS AND ANSWERS GRADED A+




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

FMOC Chemical Synthesis - ANS✔✔--Used in synthesis of a growing amino acid
chain to a polystyrene bead. FMOC is used as a protecting group on the N-terminus.
Collagen - ANS✔✔--Repeating sequence of Gly-X-Pro. 3 stranded "coiled coil".
Contains gly core.

Myoglobin 4° Structure - ANS✔✔--Symmetric homodimer,

Salting Out (Purification) - ANS✔✔--Changes soluble protein to solid precipitate.
Protein precipitates when the charges on the protein match the charges in the solution.

,Size-Exclusion Chromatography - ANS✔✔--Separates sample based on size with
smaller molecules eluting later.

Ion-Exchange Chromatography - ANS✔✔--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 - ANS✔✔--Beads are coated with a
carbon chain. Hydrophobic proteins stick better. Elute with non-H-bonding solvent
(acetonitrile).

Affinity Chromatography - ANS✔✔--Attach a ligand that binds a protein to a bead.
Elute with harsh chemicals or similar ligand.
Low-Spin Fe - ANS✔✔--Electrons are less "spread out" and are compacted by
electron rich porphyrin ring.

T-State - ANS✔✔--Heme is in high-spin state. H2O is bound to heme.

R-State - ANS✔✔--Heme is in low-spin state. O2 is bound to heme.

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

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

Isoelectric Focusing - ANS✔✔--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) - ANS✔✔--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) - ANS✔✔--Reduces disulfide bonds.

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

Homologs - ANS✔✔--Shares 25% identity with another gene

Orthologs - ANS✔✔--Similar genes in different organisms

, Paralogs - ANS✔✔--Similar "paired" genes in the same organism
.

α-helices - ANS✔✔--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 - ANS✔✔--Formed from added dipole moments of all hydrogen bonds in
an α-helix. N-terminus is δ+ and C-terminus is δ-.

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

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

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

ß-turns - ANS✔✔--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 - ANS✔✔--Not highly structured. Not necessary highly flexible, but can
occasionally move. Very variable in sequence.

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

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

ß-mercaptoethanol - ANS✔✔--Breaks disulfide bonds.

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

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

α/ß Protein Folding - ANS✔✔--Less distinct areas of α and ß folding.

α+ß Protein Folding - ANS✔✔--Two distinct areas of α and ß folding.

Mechanism of Denaturants - ANS✔✔--Highly soluble, H-binding molecules. Stabilize
protein backbone in water. Allows denatured state to be stabilized.

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