2. Cell Chemistry & Cell Components

The peptide bond is __________.

The α helix and β pleated sheet represent which level of protein structure?

Protein molecules are polymers (chains) of __________.

What do Alzheimer's, Parkinson's, and mad cow disease have in common?

The "primary structure" of a protein refers to __________.

What type of bond is directly involved in the formation of an α-helix?a. peptide bonds between amino acid residuesb. hydrogen bonds between amino acid residuesc. van der Waals interactions between nonpolar residuesd. disulfide bonds between cysteine residues

What type of information is used to direct different polypeptides to fold into different shapes?

The structural level of a protein least affected by a disruption in hydrogen bonding is thea. primary level.b. secondary level.c. tertiary level.d. quaternary level.

If a cell were to use only 10 of the 20 possible amino acids, how much effect would you expect this to have on protein diversity? Calculate and compare the number of different sequences that can be generated by randomly assembling either 10 or 20 amino acids into peptides that are five residues long.

Explain how molecular chaperones facilitate protein folding in many different polypeptides, each with their own specific shape.

Different proteins are composed of different sequences of .a. sugars;b. lipids;c. fats;d. amino acids;e. carbohydrates

Why are proteins not considered to be a good candidate for the first living molecule?a. Their catalytic capability is not sufficient for most biological reactions.b. Their amino acid monomers were not likely present in the prebiotic soup.c. They cannot serve as a template for replication.d. They could not have polymerized from amino acid monomers under early Earth conditions.

Predict the effect on protein function if each polypeptide adopted only a single, inflexible shape based on its primary structure.

Proteins may function as .a. genetic material;b. cholesterol molecules;c. fat reserves;d. enzymes;e. all of the above

Based on what you know of the peptide bonds that link together amino acid residues, why would proline's side chain reduce the flexibility of the backbone?