why does a deletion mutation usually cause more defects during protein synthesis than a point mutation?

Deletion mutation may cause a shift of base sequence, causing the reading frames for base sequence to change during translation. This may affect the type of amino acid it the original base sequence codes for, resulting in a change in amino acid sequence in the polypeptide translated. Therefore, affecting the whole protein itself. There may be wrong amino acids that prevents vital bonds like disulfide bridges to form, resulting in a huge change in 3 dimensional conformation of the protein. A point mutation may result in a gene sequence being edited. However, only the target sequence is being mutated. The rest of the gene sequences are left untouched. Therefore, the impact is localised. This ensures that even though a few wrong amino acids may be in the polyleptide, most of the bonds that are crucial for the correct 3 dimensional conformation is still present, therefore, lesser defects will be resulted due to point mutation as compared to deletion mutation.

Explanation:

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