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

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

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

What two functional groups are bound to the central carbon of every free amino acid monomer?a. an R-group and a hydroxyl groupb. an N—H group and a ═(C═O) groupc. an amino group and a hydroxyl groupd. an amino group and a carboxyl group

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

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