2 Biochemistry MC Questions - Protein Structure, Enzymes

In summary, Hemoglobin consists of 4 subunits, each with a different primary structure, and primary structure determines shape of proteins. A peptide bond is a covalent bond, but not every covalent bond is a peptide bond! And what actually is meant by an R-group? - is it part of a peptide bond?
  • #1
Atu
3
0
1. A substrate molecule may be bound to the active site of an enzyme by all of the following EXCEPT
A. Hydrogen Bonds
B. Peptide Bonds
C. Ionic Bonds
D. Van der Waals Interactions
E. Hydrophobic Interactions

2. Which of the following components is the most important in determining the 3-D structure of Hemoglobin?
A. Quaternary Structure
B. Tertiary Structure
C. Secondary Structure
D. Primary Structure
E. Number of Disulfide Bonds

For question 1, I'm between Peptide (B) and Van der Waals Interactions (D). For 2, I'm between Quaternary (A) and Primary (D).
 
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  • #2
For question 1, my sources indicate that hydrogen, Ionic, and Hydrophobic interactions all play a role, but don't mention peptide or van der Waals at all. I'm thinking that maybe peptide bonding is present, as it involves proteins (the enzyme); therefore, the answer is van der Waals. However, van der Waals can also be present, because it is a weak interaction between "close" molecules.

For Question 2, I know that Hemoglobin consists of 4 subunits (thus Quaternary Structure); however primary structure determines shape of proteins...
 
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  • #3
Hint: enzyme and the substance that attaches to the active site are two different (separate) molecules.
 
  • #4
Borek said:
Hint: enzyme and the substance that attaches to the active site are two different (separate) molecules.
That would imply that Peptide bonds are not present in active site binding, as it would form a completely new molecule, correct?

However, according to my textbook, sometimes an active site directly participates in a chemical reaction by having the R-group bond covalently to the substrate. And since a peptide bond is a covalent bond, I don't know...
 
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  • #5
Atu said:
That would imply that Peptide bonds are not present in active site binding, as it would form a completely new molecule, correct?

However, according to my textbook, sometimes an active site directly participates in a chemical reaction by having the R-group bond covalently to the substrate. And since a peptide bond is a covalent bond, I don't know...
A peptide bond is a covalent bond, but not every covalent bond is a peptide bond! And what actually is meant by an R-group? - is it part of a peptide bond?

I suggest you flip the pages forward in your book to where some enzymatic mechanisms are treated to see what is meant by 'participates in a chemical reaction by having the R-group bond covalently to the substrate' in some examples showing what is meant by this straightforward idea rather than be content with this vague general description or be drawn into essentially verbal quizzes.
 

Related to 2 Biochemistry MC Questions - Protein Structure, Enzymes

1. What is the primary structure of a protein?

The primary structure of a protein is its linear sequence of amino acids, which are joined together by peptide bonds. This sequence is determined by the genetic code encoded in the DNA of the organism.

2. How does the primary structure of a protein determine its function?

The specific sequence of amino acids in a protein determines its unique three-dimensional shape, which is crucial for its function. The sequence also influences the protein's chemical properties, such as its ability to bind to other molecules.

3. What is the secondary structure of a protein?

The secondary structure of a protein refers to the local folding patterns that occur within a polypeptide chain. These structures are stabilized by hydrogen bonds between amino acids and typically include alpha helices and beta sheets.

4. How do enzymes catalyze biochemical reactions?

Enzymes are proteins that act as catalysts in biochemical reactions, speeding up the reaction without being consumed in the process. They do so by binding to specific substrates and bringing them into close proximity, reducing the activation energy required for the reaction to occur.

5. Can the three-dimensional structure of a protein change?

Yes, the three-dimensional structure of a protein can change through processes such as denaturation or renaturation. Denaturation occurs when a protein loses its shape and function due to extreme conditions such as high temperature or pH. Renaturation is the process of a denatured protein regaining its original structure and function.

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