1.4 PROTEIN

The monomer of proteins are

• GLUCOSE

• AMINO ACID

• FATTY ACID

• PEPTIDES

The unique characteristic of each amino acid is determined by

• Its R group.

• Its amino group

• The type of peptide bond.

• Its position on the polypeptide chain

A polypeptide chain usually begins with a free amino acid group (N-terminal) and ends with a free carboxyl group(C-terminal). In theory, how many peptide bonds that can be formed from the condensation of 20 amino acids?

• 20

• 21

• 19

• 18

All of the following are considered “weak” interactions in proteins, except:

• Hydrogen bonds

• Ionic bonds

• Peptide bonds

• van der Waals forces

The primary structure of protein represents

• Helical structure of protein.

• Folded structure of protein

• 3-dimensional structure of protein.

• Linear sequence of polypeptide joined by peptide bonds.

A dipeptide has

• 2 amino acids & 1 peptide bonds.

• 2 amino acids & 2 peptide bonds.

• 3 amino acids and 3 peptide bonds.

• 2 amino acids & 4 peptide bonds.

Tertiary structure is maintained by

• Ionic bond

• Hydrogen bond

• Disulfide bridge

• All are correct

Myoglobin is a

• Protein with primary structure

• Protein with secondary structure.

• Protein with tertiary structure

• Protein with quaternary structure.

These are the factors affecting protein structures except

• High temperature

• Extreme pH

• Very low pH

• Optimum pH

Which of this bond is not found in tertiary level of protein?

• Hydrophobic interactions

• Disulfide bridge

• Ester bond

• Ionic bond