Which is an appropriate statement of involvement of the hydrophobic effect in protein folding? A) Nonpolar portions interact with polar portions in the interior of the protein. B) Nonpolar portions of the molecule associate with one another in the interior of the protein. C) Nonpolar portions of the molecule can be placed on the surface of the molecule only if hydrogen bonded to water. D) Polar portions of the molecule are generally exposed to solvent to interact effectively with water.
Which is an appropriate statement of involvement of the hydrophobic effect in protein folding? A) Nonpolar portions interact with polar portions in the interior of the protein. B) Nonpolar portions of the molecule associate with one another in the interior of the protein. C) Nonpolar portions of the molecule can be placed on the surface of the molecule only if hydrogen bonded to water. D) Polar portions of the molecule are generally exposed to solvent to interact effectively with water.
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Transcribed Image Text:Which is an appropriate statement of involvement of the hydrophobic effect in
protein folding?
A) Nonpolar portions interact with polar portions in the interior of the protein.
O
B) Nonpolar portions of the molecule associate with one another in the interior
of the protein.
OC) Nonpolar portions of the molecule can be placed on the surface of the
molecule only if hydrogen bonded to water.
OD) Polar portions of the molecule are generally exposed to solvent to interact
effectively with water.
Expert Solution

Step 1
Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids contain amino group and carboxyl group along with R side chain. The R side chain defines the characteristics of amino acid and so the overall structure of protein. Based on these R groups amino acids are classified into aliphatic, aromatic, hydrophilic and hydrophobic
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