Proteins

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1

Proteins have many functions. Which of the following can be functions of proteins?

I. Enzymes

II. Transcriptional regulators

III. Structural proteins

IV. Hormones

I, II, III, and IV

I, III, and IV

I and II

I, II, and III

I, III, IV

Explanation

Proteins serve all of these functions and many more. Most enzymes are proteins, which help to catalyze spontaneous reactions. Ribozymes can also serve this function but are instead made out of RNA. Proteins can act as transcriptional regulators which can turn on or off gene transcription. Structural proteins, such as actin, can help to maintain the shape of a cell. Other small proteins, such as insulin, can act as hormones which can diffuse throughout the body relaying important messages.

2

Proteins have many functions. Which of the following can be functions of proteins?

I. Enzymes

II. Transcriptional regulators

III. Structural proteins

IV. Hormones

I, II, III, and IV

I, III, and IV

I and II

I, II, and III

I, III, IV

Explanation

Proteins serve all of these functions and many more. Most enzymes are proteins, which help to catalyze spontaneous reactions. Ribozymes can also serve this function but are instead made out of RNA. Proteins can act as transcriptional regulators which can turn on or off gene transcription. Structural proteins, such as actin, can help to maintain the shape of a cell. Other small proteins, such as insulin, can act as hormones which can diffuse throughout the body relaying important messages.

3

Ionic bonds, disulfide bridges, hydrogen bonds and hydrophobic interactions are all examples of protein                      structure.

tertiary

primary

secondary

quaternary

None of these

Explanation

Ionic bonds, disulfide bridges, hydrogen bonds and hydrophobic interactions are all examples of protein tertiary structure when they occur within a single polypeptide chain. However, if these interactions were to occur between separate polypeptide chains then they would be defining the quaternary structure of the protein. The linear sequence of amino acids within a protein makes up the primary structure. Protein secondary structure is defined by the localized three-dimensional structure of amino acids. These localized structures are normally constructed through hydrogen bonding networks. Alpha helices and Beta pleated sheets are examples of secondary structures.

4

Ionic bonds, disulfide bridges, hydrogen bonds and hydrophobic interactions are all examples of protein                      structure.

tertiary

primary

secondary

quaternary

None of these

Explanation

Ionic bonds, disulfide bridges, hydrogen bonds and hydrophobic interactions are all examples of protein tertiary structure when they occur within a single polypeptide chain. However, if these interactions were to occur between separate polypeptide chains then they would be defining the quaternary structure of the protein. The linear sequence of amino acids within a protein makes up the primary structure. Protein secondary structure is defined by the localized three-dimensional structure of amino acids. These localized structures are normally constructed through hydrogen bonding networks. Alpha helices and Beta pleated sheets are examples of secondary structures.

5

Which of the following is not typical of an enzyme?

It increases the amount of products made

It increases the rate of a reaction

It orients the substrates so they can react

It lowers the activation energy of a reaction

Explanation

Enzymes are used to increase the rate of a reaction. This is accomplished by lowering the activation energy required for substrates to react, often by altering the transition state. Enzymes do not, however, increase the amount of products formed; they simply help the equilibrium be reached more quickly. In other words, enzymes change the rate of a reaction, but not the equilibrium.

6

Which of the following is not typical of an enzyme?

It increases the amount of products made

It increases the rate of a reaction

It orients the substrates so they can react

It lowers the activation energy of a reaction

Explanation

Enzymes are used to increase the rate of a reaction. This is accomplished by lowering the activation energy required for substrates to react, often by altering the transition state. Enzymes do not, however, increase the amount of products formed; they simply help the equilibrium be reached more quickly. In other words, enzymes change the rate of a reaction, but not the equilibrium.

7

How do enzymes speed up reactions?

By lowering the activation energy required to begin the reaction

By providing additional energy to the system

By altering the net change in free energy of the reaction

By increasing the substrate concentration

Explanation

Enzymes speed up reactions by lowering the energy required to begin the reaction (the activation energy). They do not have any direct effect on the change in free energy, nor do they provide extra energy to the system. Enzymes also cannot alter the substrate concentration. Catalytic action will never be able to influence the equilibrium constant or equilibrium concentrations of a reaction.

8

How do enzymes speed up reactions?

By lowering the activation energy required to begin the reaction

By providing additional energy to the system

By altering the net change in free energy of the reaction

By increasing the substrate concentration

Explanation

Enzymes speed up reactions by lowering the energy required to begin the reaction (the activation energy). They do not have any direct effect on the change in free energy, nor do they provide extra energy to the system. Enzymes also cannot alter the substrate concentration. Catalytic action will never be able to influence the equilibrium constant or equilibrium concentrations of a reaction.

9

The Gila monster, H. suspectum, produces a neurotoxic venom containing helothermine, which causes lethargy and partial paralysis of the limbs. Considering that this toxin partially inhibits voluntary muscle contraction, which of the following is the most likely mechanism?

It inhibits channels in the cerebellum

It blocks gates in striated muscle cells

It attacks neural synapses in the brain stem

It degrades myelin sheaths in the motor cortex

It inhibits acetylcholine transmission in the spinal cord

Explanation

Helothermine is a peptide toxin that inhibits calcium channels in the cerebellar granule cells. The cerebellum is the part of the brain that controls voluntary muscle movements such as those in the limbs, and the toxin must be inhibiting very specifically to cause those two symptoms and not total paralysis or other problems.

10

Which of the following statements about the general roles and properties of biological enzymes is not true?

Enzymes are consumed and depleted over the course of a reaction.

Enzymes increase the reaction rate.

Enzymes lower the activation energy of a reaction.

Enzymes do not alter the equilibrium of the reaction.

Biological catalysts do not have to be proteins.

Explanation

Enzymes are not consumed or used up during a reaction, rather they simply increase the rate of reaction by making it "easier" for the reaction to occur, i.e. lowering the activation energy. Equilibrium is not altered by the presence of an enzyme. There are examples of catalytic RNA molecules (ribosomes) and therefore biological catalysts are not always proteins.

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