Leucine Zipper shown below is an example of a coiled coil A

Last updated: 1/20/2024

Leucine Zipper shown below is an example of a coiled coil A typical Leucine Zipper consists of two a helixes with leucine residues in about 7 residue intervals Shown below is one of those intervals In Biochemistry mutations often are done to study the effect of changing residues in a protein Electrostatic reactions are where a positively charged side chain interacts with a negatively charged side chain like the one shown below lysine s positive side chain interacting with glutamate s negative side chain 0 Potential cons Potential electrostatic interactions Gly f Instructions Prompt 1 Explain what principles are involved in holding the two a helices together Suggest one possible residue that could replace leucine as indicated by the red star and maintain the hydrophobic core shown below and suggest one possible residue that would destabilize the core Please explain your reasoning Glu b Glu Class ww d Hydrophobic core Potential electrostatic interactions Potential electrostatic Lys Glu Gly