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Phosphorylation of serines, threonines or tyrosines often affects protein function. For example, many kinases are themselves...

Phosphorylation of serines, threonines or tyrosines often affects protein function. For example, many kinases are themselves activated by phosphorylation. Why do you think addition of a phosphate group on these amino acids affects the function of a protein? Can you think of a way to test your idea by mimicking the effect of phosphorylation (hint: think about the side groups on different amino acids)?

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Answer #1

Phosphorylation is the process by which a phosphoryl group (hydrophilc)is introduced to an organic molecule ; in this case an amino acid.

When phosphorylating an amino acid the side chain becomes charged , this chemical change will facilitate changes such as modification in the folding patterns of amino acids and also interaction with the adjacent ones leading to activation or deactivation of these molecules by conformational or related changes .

This is crucial in the various regulatory mechanisms in the cells which includes signal transmission , energy production etc..

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