Protein Z is a protein which is phosphorylated at Ser-120. The functional role of this phosphorylation...

Protein Z is a protein which is phosphorylated at Ser-120. The functional role of this phosphorylation site

in protein Z was assessed by site-directed mutagenesis. Mutation of Ser-120 to Asp resulted in a protein that

is unable to function, while mutation to Ala resulted in a protein with increased ability to function. Discuss a

structural basis for these observations.

Solutions

Expert Solution

Majority of the proteins are phosphorylated and regulates its function. The most common phosphorylated amino acid in protein are serine, threonine, and tyrosine. The phosphorylation of amino acid residue introduces a charge in the protein, making a hydrophilic in nature which alters the interaction of that protein with nearby proteins. The addition of a phosphate group in non-charged amino acids can result in the alteration of a hydrophobic region of the protein into an extremely hydrophilic portion of the protein. Therefoer, the protein dynamics can result in a conformational change in the structure of the protein and thereby regulating the function.

In the given observation, first Ser-120, the site for phosphorylation is mutated into Asp, which contains -COOH as R group. The conversion of the Ser to Asp can result in no change in charge of the region. however, mutation of Ser to Ala, a non-charged amino acid will result in the conversion of the hydrophilic site as hydrophobic resulting in an alteration of protein function.

gladiator answered 1 year ago

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