Consider the structure of Cro repressor protein from bacteriophage lambda. It is a DNA binding protein, and like many sequence-specific DNA binding proteins, it must function as a homodimer.Notice the mutual docking of a phenylalanine residue from each subunit into a hydrophobic pocket of the partner subunit. These hydrophobic interactions are required for dimerization.The noncovalent interactions highlighted in yellow are also required for dimerization. These interactions represent examples of:- secondary structure- tertiary structure- quaternary structure- secondary AND quaternary structure- tertiary AND quaternary structure (selected)**Image Description:**The image shows a graphical representation of a dimerized Cro repressor protein with two different colored subunits, red and green. The protein structure illustrates helical regions and interactions within a blue highlighted area, suggesting noncovalent interactions necessary for the dimerization of the protein. The phenylalanine residues are docked into opposing hydrophobic pockets, highlighted in yellow, indicating their crucial role in stabilization. The selected answer is "tertiary AND quaternary structure," indicating these interactions pertain to both levels of protein structuring.

Name: Consider the structure of Cro repressor protein from bacteriophage la
Uploaded: 2024-03-20T06:42:41.000Z
Channel: Bartleby
Description: Consider the structure of Cro repressor protein from bacteriophage lambda. It is a DNA binding protein, and like many sequence-specific DNA binding proteins, it must function as a homodimer.Notice the mutual docking of a phenylalanine residue from e