Multiple or none of the answers may be correct: The affinity of a protein for a

Question

Multiple or none of the answers may be correct:

The affinity of a protein for a ligand

Changes as a function of the ligand concentration

Is described by the Kd

Is governed at the molecular level by weak interactions between the protein’s amino acids and the functional groups on the ligand

Is a measure of the tightness of the binding interaction

The following statements about enzyme inhibitors are TRUE:

Mixed inhibitors bind at a second site

Competitive inhibitors bind at the active site

Suicide inhibitors irreversibly (covalently) attach to the active site

Uncompetitive inhibitors bind at the active site

The following statements about protein secondary structure are TRUE:

Beta sheets may have parallel or anti-parallel strands

Alpha helices are always right-handed

Beta sheets form hydrogen bonds between the carbonyl groups on one strand and the carbonyl groups on the opposite strand

Alpha helices are always stabilized by interactions between parallel helices

Changes as a function of the ligand concentration

Is described by the Kd

Is governed at the molecular level by weak interactions between the protein’s amino acids and the functional groups on the ligand

Is a measure of the tightness of the binding interaction

Explanation / Answer

affinity of a protien for a ligand does not change with concentration is does not descriced by Kd and is not governed at the molecular level by weak interactions between the protein’s amino acids and the functional groups on the ligand.

1-D

mixed inhibitors bind to a allosteric sites i.e a site different from the active site

Competitive inhibition is a form of enzyme inhibition where binding of the inhibitor to the active site on the enzyme prevents binding of the substrate and vice versa.

2--B

The -sheet (also -pleated sheet) is a common motif of regular secondary structure in proteins. Beta sheets consist of beta strands (also -strand) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A -strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of -sheets has been implicated in formation of the protein aggregates and fibrils observed in many human diseases, notably the amyloidoses such as Alzheimer's disease.

3-C

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