Answer:
C. Trp D. Phe E. Tyr
Explanation:
The concentration of a protein has a direct relation with absorbance of the protein in a UV spectrophotometer. The formula which relates concentration with absorbance is described as under:
A = ∈ x c x l
where, A = Absorbance
∈ = Molar extinction co-efficient
c = Concentration of absorbing species i.e. protein
l = Path length of light
Tryptophan (Trp), phenylalanine (Phe ) and tyrosine (Tyr) are three aromatic amino acids which are used to measure protein concentration by UV. It is mainly because of tryptophan (Trp), protein absorbs at 280 nm which gives us an idea of protein concentration during UV spectroscopy.
The table depicting the wavelength at which these amino acids absorb and their respective molar extinction coefficient is as under:
Amino acid Wavelength Molar extinction co-efficient (∈)
Tryptophan 282 nm 5690
Tyrosine 274 nm 1280
Phenylalanine 257 nm 570
In view of table above, we can easily see that Molar extinction co-efficient (∈) of Tryptophan is highest amongst all these 3 amino acids that is why it dominates while measuring concentration.
<span>The correct answer is 3: 0.10 M K3PO4(aq). The higher the concentration (or molarity), the higher the boiling point. Thus, the solution with the most moles will have the highest boiling point. SO4, PO4, and NO3 are all polyatomic ions, so by definition, they only have one mole. In K3PO4, K3 has 3 moles and PO4 has 1 mole, meaning all together it has 4 moles (more than any of the other options).</span>
Explanation:
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Mutation affects can be different just with changes as small as the substitution of a single DNA building block or nucleotide base with another nucleotide base
