question archive 1)When proteins absorb light in the 250 nm to 320 nm range, most of this absorbance is caused by three aromatic amino acids: phenylalanine, tyrosine, and tryptophan
1)When proteins absorb light in the 250 nm to 320 nm range, most of this absorbance is caused by three aromatic amino acids: phenylalanine, tyrosine, and tryptophan
Subject:BiologyPrice: Bought3
1)When proteins absorb light in the 250 nm to 320 nm range, most of this absorbance is caused by three aromatic amino acids: phenylalanine, tyrosine, and tryptophan. Only one of the above-mentioned amino acids responds to added NaOH at the concentration we used. Which one?
2)Hand-draw the chemical reaction that accounts for the spectral change of this amino acid in the 250 nm to 320 nm region upon addition of NaOH.
3The molar extinction coefficient for the peak of the GFP chromophore in strong base is 44,100 L/mol-cm. Use the Beer-Lambert Law to calculate the molarity of the diluted GFP solution. Show work
4)Use the Beer-Lambert Law to calculate the molar extinction coefficient for GFP in Tris buffer at 397 nm (or the peak you observed closest to 397 nm). show work
5)Estimate the molar extinction coefficient (ε) for Brilliant Yellow at λmax. Remember that the units for ε in the Beer-Lambert equation are L/mol*cm, so will have to make conversions before estimating ε. The molecular weight of Brilliant Yellow is 624.55 g/mol. Please show work.
6)Imagine that there is a solution of Brilliant Yellow of unknown concentration. After measure its absorbance at using the exact same procedure we use in this lab, and obtain a reading of 2.235. Explain why it is impossible to calculate the concentration of this solution without first diluting the sample
