biochem exam 2

biochem exam 2

University

97 Qs

quiz-placeholder

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biochem exam 2

biochem exam 2

Assessment

Quiz

Chemistry

University

Easy

Created by

Mary Posadas

Used 1+ times

FREE Resource

97 questions

Show all answers

1.

MULTIPLE CHOICE QUESTION

2 mins • 1 pt

Hydrogen bonding helps to stabilize all of the structural levels of protein except for...

Primary structure

Secondary structure

Tertiary structure

Quaternary structure

Quaternary structure

2.

MULTIPLE CHOICE QUESTION

2 mins • 1 pt

The hydrophobic effect helps to stabilize which of the structural levels of protein below?

Primary structure

Secondary structure

Tertiary structure

Quaternary structure

Tertiary & Quaternary

3.

MULTIPLE CHOICE QUESTION

2 mins • 1 pt

Which of the following is true for both alpha helices and beta sheets?

Formation of these motifs are enthalpically stabilized by hydrogen bonding

Compared to unfolded polypeptides, their formations are entropically unfavored.

Formation of these motifs are enthalpically stabilized by the hydrophobic effect.

All of above

4.

MULTIPLE CHOICE QUESTION

2 mins • 1 pt

True or false: Tertiary and quaternary structure are never stabilized by covalent bonds

True

False

5.

MULTIPLE CHOICE QUESTION

2 mins • 1 pt

Which of the following is the least likely to denature a protein?

Addition of sodium dodecyl sulfate to the protein solution

Boiling the protein solution

Addition of 10 M NaOH to the protein solution

Addition of benzene to the protein solution.

Addition of 1 M NaCl to the protein solution

6.

MULTIPLE CHOICE QUESTION

2 mins • 1 pt

Which of the following provide no enthalpic contribution to the stability of the 3D structure of a protein?

Hydrophobic effect

Disulfide bonds

London’s forces

Dipole-dipole interactions

Ion-dipole interactions

7.

MULTIPLE CHOICE QUESTION

2 mins • 1 pt

What concentration of ligand ([L]) is needed for 80. % of the binding sites to bind ligand if the Kd for ligand binding is 500 μM? The protein is a homodimer that exhibits no cooperativity between binding sites.

250 μM

500 μM

2000 μM

200,000 μM

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