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How many moles of CH₃NH₃Cl  need to be added to 200.0 mL of a 0.500 M solution of CH₃NH₂ (Kb for CH₃NH₂ is 4.4 × 10⁻⁴) to make a buffer with a pH of 11.00?

If the concentration at which half of the receptors in a protein’s active site are bound is 1.5M, what is the KD for that protein?

What is a Buffer? What is a Buffer made of? Using an example, describe how a buffer works chemically.

If the value of KD is 2.1 what will be the concentration of ligand needed to bind half of the protein’s active site?

Define the terms Dextrorotary and Levorotary and how the terms are used in relationship to amino acids.

Arrange the steps involved in folding of globular proteins into a proper sequence. A. “Molten globule” formation of assembled domains. B. Formation of domains through cooperative aggregation of folding nuclei. C. Adjustment in the conformation of domains. D. Rapid and reversible formation of local secondary structure. E. Final protein monomer formation. Place the letter of the steps in order without spacing Ex. ABCDE [order] If the following section of a polypeptide is folded into an α-helix, to which amino acid is the carbonyl group of alanine hydrogen bonded? ala-ser-val-asp-glu-leu-gly [AA]

  Using the graph above, Designate the pKa values for the Amino Acid: pKa of the Carboxyl Group = [carboxyl] pKa of the Amine Group = [amine] pKa of the Side Chain = [side] Based on the table below, what is the identity of this Amino Acid? [AA]  

Describe in detail what a hydrogen bond is and how it is formed.  Give 3 examples of where hydrogen bonding plays a key role in biochemical structure and function.

For the amino acid shown below, describe the structure in terms or R,S and D,L and detail out how you know these features.  

  For each of the letters A-G above, select the correct protein stabilization they depict: A = [A] ; B = [B] ; C = [C] ; D = [D] ; E = [E] ; F = [F] ; G = [G]