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Biochem ACS Review Exam Questions And Answers (Guaranteed A+)

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  • ACS Biochemistry
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  • ACS Biochemistry

©FYNDLAY EXAM SOLUTIONS 2024/2025 ALL RIGHTS RESERVED. 1 | P a g e Biochem ACS Review Exam Questions And Answers (Guaranteed A+) What amino acids have nonpolar, aliphatic R groups? - answerGlycine, Alanine, Proline, Valine, Leucine, Isoleucine, Methionine What amino acids have polar, unchar...

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  • November 28, 2024
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  • 2024/2025
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  • ACS Biochemistry
  • ACS Biochemistry
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©FYNDLAY EXAM SOLUTIONS 2024/2025

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Biochem ACS Review Exam Questions And
Answers (Guaranteed A+)


What amino acids have nonpolar, aliphatic R groups? - answer✔Glycine, Alanine, Proline,
Valine, Leucine, Isoleucine, Methionine

What amino acids have polar, uncharged R groups? - answer✔Serine, Threonine, Cysteine,
Asparagine, and Glutamine

What amino acids have aromatic R groups? - answer✔Phenylalanine, Tyrosine, and Tryptophan

What amino acids have negatively charged R groups? - answer✔Aspartate and Glutamate

What amino acids have positively charged R groups? - answer✔Lysine, Arginine, and Histidine

What is isoelectric focusing? - answer✔Proteins are electrophoresed in a pH gradient gel. Each
protein will move in the gel as long as the protein contains a charge

What does SDS do? - answer✔It binds to proteins and denatures it. All proteins have same
mass/ charge ratio

How do you determine the Amino Terminus? - answer✔1. Make a derivative of the N-terminus
with a marker molecule
2. Hydrolyze the peptide
3. N-terminal AA is identified by chromatography- modified amino acid will elute differently
than unmodified AA

What molecule does Edman Degradation use? - answer✔Phenyl Isothiocyanate (PTH)

What does Edman Degradation do? - answer✔It removes one amino acid at a time. The limit is
50 amino acids. After 50 amino acids, the polypeptide must be hydrolyzed into smaller fractions

Where does Cyanogen Bromide cleave? - answer✔Cleaves only on the caryboxyl side of
Methionine residues

Where does Trypsin cleave? - answer✔Trypsin cleaves on the carboxyl side of positive residues
such as Arginine and Lysine


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, ©FYNDLAY EXAM SOLUTIONS 2024/2025

ALL RIGHTS RESERVED.
What happens in Disulfide Position? - answer✔It is a diagonal electrophoresis.
The peptides are cleaved without destroying the disulfide bonds and then exposed to performic
acid vapors.
The performic acid vapors convert any S-X bond to a SO3-.
These fragments will be off the diagonal

In Peptide Synthesis, what is the protecting group? - answer✔Fmoc

What is the group that activates amino acid 2? - answer✔DCC- Dicyclohexylcarbodiimide

What acts as the nucleophile in Peptide Synthesis? - answer✔Amino acid 1 that is connected to
the polystyrene bead.

What causes the polystyrene bead to disconnect from amino acid 1? - answer✔HF

In what order does peptide synthesis, synthesize amino acids? - answer✔Carboxy end to the
amine end

In what order does the body synthesize amino acids? - answer✔Amino terminus to carboxy
terminus

What are the hydrogen bonds in Alpha Helix? - answer✔The carboxyl group is hydrogen
bonded with the Hydrogen on the Nitrogen 4 residues away. Alpha helix is clockwise, or right
handed

Which Beta Pleated sheet is more stable, parallel or antiparallel? - answer✔Antiparallel,
because there is a direct overlap of electrons which creates more stability

What does B-mercaptoethanol do? - answer✔It breaks disulfide bonds

What does Urea do? - answer✔It interrupts hydrogen bonds

What is Levinthal's Paradox? - answer✔It is the difference between the calculated time for a
protein to fold and the real time it take for a protein to fold.

The discrepancy in time is answered by what? - answer✔Progressive stabilization

What is Progressive stabilization? - answer✔It is the stabilization of intermediates that
resemble parts of the final folded state

What is the molten globule state? - answer✔It is the state between random coil and native
state. It contains much secondary structure.

How is the molten globule formed? - answer✔It is formed by hydrophobic collapse.
Hydrophobic residues are sequestered toward the inside of a protein


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