The amino acid glycine is often used as a component of buffers in biochemical experiments. The amino group of glycine has a pKa of 9.6, which can exist in the protonated form -NH₃⁺ or the free base -NH₂ as shown in this equilibrium:

        R-NH₃⁺ ⇌ R-NH₂ + H⁺

(a) Using glycine as a buffering agent requires specific pH ranges. Identify the buffer range for glycine’s amine group and describe how this molecule provides buffer capabilities as small amounts of HCl(aq) is added to the solution.

(b) In a 0.1 M solution of glycine at pH = 9, what fraction of glycine has its amino group in the -NH₃⁺ form?

(c) When 90% of glycine is in its -NH₃⁺ form, what is the numerical difference between the pH of the solution and the pKa of the amino group?

30.0 uM(microMolar) solution of enzyme catalyzed breakdown of 0.250M of substrate in 2 minutes. How many molecules of substrate were converted to product each second by one enzyme molecule?

1. Describe the link between understanding enzyme mechanism and drug design and development.

2. How does regulation of 1 enzyme in a metabolic pathway modulate the flux through the entire pathway?

25) Am enzyme-catalyzed reaction proceeds at a faster rate than an uncatalyzed reaction because the enzyme lowers the difference in free energy between the reactants and the products.
a. True
b. False

Using Ellman’s reagent, find the number of cysteines in a protein that has a concentration of 30 mg/ml solution with a molecular weight of 15,000 Da. Data-- 0.1 ml of the protein was reacted with the reagent and diluted to 10 ml and the absorbance at 412 nm was 1.4 A. Hint, first find the moles of protein used for the experiment, then calculate the moles of Ellman’s reagent that reacted

DA=34.9 DL=15.94 DGAP=18.96

use these duration values to calculate the for the predicted changes in the banks assets a. a decrease in .35 percent on interest rates on assets

b for a .5 percent decrease in interest rates on liabilities

c. what is the change in equity value MVE from the decrease in balance sheet   calculated in part 1 and 2 in part a and b

Describe and explain observed conductivity changes during the titration of your amino acid. Which parameter is more helpful in locating the first and the second equivalence points, the pH or the electrical conductivity? The amino acid is glutamic acid (HGlu) Thank you.

1. What is the ATP yield from Glycolysis, Pyruvate processing, TCA cycle? Overall maximum theoretical yield from complete oxidation of one molecule of Glucose?