Lehninger Biochemistry Chapter 4 Questions And Answers Rated A+.
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Lehninger Biochemistry Chapter 4
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Lehninger Biochemistry Chapter 4
Lehninger Biochemistry Chapter 4 Questions And Answers Rated A+.
All of the following are considered "weak" interactions in proteins, except:
A) hydrogen bonds.
B) hydrophobic interactions.
C) ionic bonds.
D) peptide bonds.
E) van der Waals forces. - correct answer. D) p...
Lehninger Biochemistry Chapter 4
Questions And Answers Rated A+.
All of the following are considered "weak" interactions in proteins, except:
A) hydrogen bonds.
B) hydrophobic interactions.
C) ionic bonds.
D) peptide bonds.
E) van der Waals forces. - correct answer. D) peptide bonds.
The most important contribution to the stability of a protein's conformation appears to be
the:
A) entropy increase from the decrease in ordered water molecules forming a solvent
shell around it.
B) maximum entropy increase from ionic interactions between the ionized amino acids
in a protein.
C) sum of free energies of formation of many weak interactions among the hundreds of
amino acids in a protein.
D) sum of free energies of formation of many weak interactions between its polar amino
acids and surrounding water.
E) stabilizing effect of hydrogen bonding between the carbonyl group of one peptide
bond and the amino group of another. - correct answer. A) entropy increase from the
decrease in ordered water molecules forming a solvent shell around it.
In an aqueous solution, protein conformation is determined by two major factors. One is
the formation of the maximum number of hydrogen bonds. The other is the:
A) formation of the maximum number of hydrophilic interactions.
B) maximization of ionic interactions.
C) minimization of entropy by the formation of a water solvent shell around the protein.
D) placement of hydrophobic amino acid residues within the interior of the protein.
E) placement of polar amino acid residues around the exterior of the protein. - correct
answer. D) placement of hydrophobic amino acid residues within the interior of the
protein.
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