Question

Thr-91 of Complex I is conserved through evolution. It is crucial for the functioning of Complex...

Thr-91 of Complex I is conserved through evolution. It is crucial for the functioning of Complex I in the ETC. I make two forms of mutant yeast: one in which Thr-91 is mutated to an alanine (Thr91Ala) and another in which Thr-91 is mutated to a tryptophan (Thr91Trp).

What is the different between the mutations and what other information can I derive from this?

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Answer #1

The change of amino acid from therionine to alanine will result in change of polar amino acid to non polar which can alter the folding of protein and function also. The OH group of therionine may also be required for functioning of normal protein. The changes would affect more if both the mutations are occurring in active site of the protein. The change to tryptophan also result in same effects. The polar amino acid will change to other side chain containing amino acid.

The other information which can be derived from this is regarding codon changes and nucleotide changes in protein coding DNA sequence. Thus info can be deduced from different codons.

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