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Define and Describe the key features of Molecular Recognition and Structural Complementarity. 

For each of the structures below, name the amino acid:   [Amino1]     [Amino2]   [amino3]   [amino4]   [amino5]

Describe in detail (6 steps) the life cycle of a virus.  

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?

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

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?

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?

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]

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

  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]