100% satisfaction guarantee Immediately available after payment Both online and in PDF No strings attached
logo-home
ACS BIOCHEM ACTUAL EXAM 2024| ACS BIOCHEM BRAND NEW(VERIFIED) EXAM QUESTIONS AND CORRECT ANSWERS|ALL GRADED A+|GUARANTEED SUCCESS|LATEST UPDATE . $11.49   Add to cart

Exam (elaborations)

ACS BIOCHEM ACTUAL EXAM 2024| ACS BIOCHEM BRAND NEW(VERIFIED) EXAM QUESTIONS AND CORRECT ANSWERS|ALL GRADED A+|GUARANTEED SUCCESS|LATEST UPDATE .

 1 view  0 purchase
  • Course
  • ACS BIOCHEM
  • Institution
  • ACS BIOCHEM

ACS BIOCHEM ACTUAL EXAM 2024| ACS BIOCHEM BRAND NEW(VERIFIED) EXAM QUESTIONS AND CORRECT ANSWERS|ALL GRADED A+|GUARANTEED SUCCESS|LATEST UPDATE . Henderson-Hasselbach Equation - ANSWER-pH = pKa + log ([A-] / [HA]) FMOC Chemical Synthesis - ANSWER-Used in synthesis of...

[Show more]

Preview 3 out of 18  pages

  • October 23, 2024
  • 18
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers
  • ACS BIOCHEM
  • ACS BIOCHEM
avatar-seller
BRILLIANTSOLUTIONS
ACS BIOCHEM ACTUAL EXAM 2024|
ACS BIOCHEM BRAND NEW(VERIFIED) EXAM
QUESTIONS AND CORRECT ANSWERS|ALL
GRADED A+|GUARANTEED SUCCESS|LATEST
UPDATE 2024-2025.




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.

,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

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.

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.

α/ß Protein Folding - ANSWER-✅Less distinct areas of α and ß folding.

α+ß Protein Folding - ANSWER-✅Two distinct areas of α and ß folding.

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

Temperature Denaturation of Protein - ANSWER-✅Midpoint of reaction is Tm.

Cooperative Protein Folding - ANSWER-✅Folding transition is sharp. More
reversible.

Folding Funnel - ANSWER-✅Shows 3D version of 2D energy states. Lowest energy is
stable protein. Rough funnel is less cooperative.

Protein-Protein Interfaces - ANSWER-✅"Core" and "fringe" of the interfaces. Core is
more hydrophobic and is on the inside when interfaced. Fringe is more hydrophilic.

The benefits of buying summaries with Stuvia:

Guaranteed quality through customer reviews

Guaranteed quality through customer reviews

Stuvia customers have reviewed more than 700,000 summaries. This how you know that you are buying the best documents.

Quick and easy check-out

Quick and easy check-out

You can quickly pay through credit card or Stuvia-credit for the summaries. There is no membership needed.

Focus on what matters

Focus on what matters

Your fellow students write the study notes themselves, which is why the documents are always reliable and up-to-date. This ensures you quickly get to the core!

Frequently asked questions

What do I get when I buy this document?

You get a PDF, available immediately after your purchase. The purchased document is accessible anytime, anywhere and indefinitely through your profile.

Satisfaction guarantee: how does it work?

Our satisfaction guarantee ensures that you always find a study document that suits you well. You fill out a form, and our customer service team takes care of the rest.

Who am I buying these notes from?

Stuvia is a marketplace, so you are not buying this document from us, but from seller BRILLIANTSOLUTIONS. Stuvia facilitates payment to the seller.

Will I be stuck with a subscription?

No, you only buy these notes for $11.49. You're not tied to anything after your purchase.

Can Stuvia be trusted?

4.6 stars on Google & Trustpilot (+1000 reviews)

67096 documents were sold in the last 30 days

Founded in 2010, the go-to place to buy study notes for 14 years now

Start selling
$11.49
  • (0)
  Add to cart