Exam 1 Review Pt1

How many pKa values does lysine have?

• 1

• 2

• 3

• 4

What orientation do naturally occurring amino acids predominantly have?

• D-configuration

• L-configuration

• Racemic mixture

• Both D- and L- configurations equally

What happens when peptide bonds are broken?

• Water is consumed

• Water is released

• No change in water occurs

• ATP is produced

What is the correct order of steps for protein sequencing?

• 1. Fragment chain, 2. Separate chains, 3. Use mass spec, 4. Remove disulfide bonds, 5. Reconstruct sequence using overlaps

• 1. Use mass spec, 2. Separate chains, 3. Remove disulfide bonds, 4. Fragment chain, 5. Reconstruct sequence using overlaps

• 1. Remove disulfide bonds, 2. Fragment chain, 3. Use mass spec, 4. Separate chains, 5. Reconstruct sequence using overlaps

• 1. Separate chains, 2. Remove disulfide bonds, 3. Fragment chain, 4. Use mass spec, 5. Reconstruct sequence using overlaps

How do φ (phi) and ψ (psi) angles of a peptide bond influence protein structure?

• They freely rotate without restrictions.

• They are restricted due to steric hindrance between atoms.

• They only allow cis conformations but allow for trans conformations.

• They are fixed and do not rotate.

The function of a protein depends on its:

• Sequence

• Structure

• Solubility

• Phi/Psi angles

Tags

NGSS.HS-LS1-1

Which type of interaction primarily drives protein folding?

• Covalent bonding

• van der Waals forces

• Ionic interactions

• Hydrophobic interactions

What is the importance of Ramachandran maps in protein structure analysis?

• They predict the amino acid sequence of a protein.

• They describe the secondary structure of proteins.

• They determine the molecular weight of a protein.

• They show allowed φ (phi) and ψ (psi) angle combinations.

Which level of protein structure is primarily stabilized by hydrogen bonds?

• Primary structure

• Secondary structure

• Tertiary structure

• Quaternary structure

What is the purpose of helical capping in an α-helix?

• To prevent hydrogen bond formation on the outside of the helix

• To stabilize the helix by forming interactions at the N- and C-termini

• To disrupt the helix and promote unfolding as a stress response

• To extend the length of the helix by incorporation of beta helices at termini