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How does the modern filibuster differ from the traditional filibuster?

What does the term “filibuster” refer to in the context of the Senate?

What is a consequence of the heightened partisanship in Congress on the legislative process?

What term describes the historical difficulty of unseating an incumbent in Congress?

What is the purpose of standing committees in Congress?

What is the significance of the “necessary and proper clause” in the U.S. Constitution?

A ligand, L, binds non-covalently to the active site of an enzyme with a dissociation constant, Kd, of 1 nM. When a different type of ligand, X, is bound non-covalently to a different site in the enzyme the ligand L binds non-covalently to the active site of the enzyme with a Kd of 1 µM. The effect exerted by X on the binding of L to the enzyme is an example of:

An antibody binds specifically to a small, monomeric globular protein only when the small protein is in its denatured (i.e. unfolded) state; the antibody does not bind when the small protein is in its native (i.e. folded) state. Given only this information and what you know about the structure and properties of the amino acids, which of the following amino acids is most likely to be found in the epitope recognized by the antibody?

A ligand-receptor binding equilibrium has a Kd of 4 μM. When the free ligand concentration [L] is 2 μM, what is the fractional occupancy of the protein receptor’s binding site, θ?

Consider a hypothetical scenario in which each of the following oligopeptides is capable of folding into a stable native state in aqueous solution. When we measure the rates at which each of these oligopeptides folds starting from the denatured (i.e. unfolded) state, we find that three of them appear to fold as single populations, i.e. in these three cases, all copies of the oligopeptide appear to fold at approximately the same rate. In contrast, with the fourth oligopeptide, there appears to be two distinct populations: some copies of the oligopeptide fold rapidly, while other copies fold much more slowly. Given only this information and the sequences shown below, identify the oligopeptide sequence that is most likely to exhibit two distinct folding populations.