Consider the structure of Cro repressor protein from bacteriophage lambda B. It is a DNA binding protein, and like many sequence- specific DNA binding proteins, it must function as a homodimer Ex. 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 O tertiary structure Oquaternary structure O secondary AND quaternary structure tertiary AND quaternary structure

Consider the structure of Cro repressor protein from bacteriophage lambda B. It is a DNA binding protein, and like many sequence- specific DNA binding proteins, it must function as a homodimer Ex. 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 O tertiary structure Oquaternary structure O secondary AND quaternary structure tertiary AND quaternary structure

Name: Consider the structure of Cro repressor protein from bacteriophage la
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Description: Consider the structure of Cro repressor protein from bacteriophage lambda E. It is a DNA binding protein, and like many sequence-specific DNA binding proteins, it must function as a homodimer Ex.Notice the mutual docking of a phenylalanine residue f

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter30: Protein Synthesis

Section: Chapter Questions

Problem 2P

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