You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole^-1 cm^-1 Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20- fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution?
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You are given a pure protein sample to characterize and provided the following information:
Its molar extinction coefficient, ε280, is 0.25 liters micromole^-1 cm^-1
Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20- fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution?
Introduction
One or more long chains of amino acid residues make up the massive biomolecules and macromolecules known as proteins. Among the many tasks that proteins carry out in living things include catalysing metabolic processes, replicating DNA, reacting to stimuli, giving cells and organisms structure, and moving molecules from one place to another.
The primary way that proteins differ from one another is in the order of their amino acids, which is determined by the nucleotide sequence of their genes and typically causes a protein to fold into a certain 3D structure that controls its activity.
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