A protein solution has ε=0.4(molar absorptivity constant) at 280nm. If we dilute the solution of the...

A protein solution has ε=0.4(molar absorptivity constant) at 280nm. If we dilute the solution of the protein 10 times what will happen to ε?

Expert Solution

Molar absorptivity of any compound is characteristic value of that particular compound/protein, it doesn’t change with the concentration of the solution, so for this particular protein ε=0.4(molar absorptivity constant) at 280nm remains same all concentrations, although absorbance of the solution will change.

Beer Laberts law can be written as,

A= εcl

Where, A= Absorbance of the solution

c= concentration of solution

l= Length of the absorbing cell

ε= Molar absorptivity constant

ε or Molar absorptivity constant is the absorbance of the solution at one molar concentration of solution, hence it remains constant for that particular compound or protein in this question at given concentrations.

queen_honey_blossom answered 2 years ago

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