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Hydrophobic interactions can be very important in determining protein shape. The

ID: 479177 • Letter: H

Question

Hydrophobic interactions can be very important in determining protein shape. They are also important in interactions between DNA-binding proteins and DNA. Which of the following is an example of a hydrophobic interaction?

Hydrophobic interactions can be very important in determining protein shape. They are also important in interactions between DNA-binding proteins and DNA. Which of the following is an example of a hydrophobic interaction?

a Alanine, glycine, and phenylalanine are positioned together. b Glutamine and tyrosine are attracted to glycine. c The nitrogenous bases of DNA are joined by hydrogen bonds. d Two cysteines form a disulfide bond.

Explanation / Answer

Ans = b

The interactions between non-polar molucules are called hydrophobic interactions.

Glutamine and tyrosine are attracted to glycine. This attraction is nothing but hydrophobic interaction.