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6. Polar charged amino acids are...

  • hydrophobic
  • carboxyl groups
  • always present in their fully charged state, and are able to form ionic bonds with other charged species within a cell.
  • amino acids

7. How many residues constitute one turn of an alpha helix?

  • An α-helix has 3.1 residues per turn.
  • An α-helix has 3.6 residues per turn.
  • 3.7 residues per turn.
  • An α-helix has 2 residues per turn.

8. Where would you likely find the most biologically active zones of a polypeptide?

  • The primary structure.
  • Portions not found in alpha helix or beta pleated sheets may be found in zones such as hinges, turns, loops and finger like extensions. These are often the most flexible sections of a polypeptide, and the sites of the greatest biological activity.
  • in the amino acid sequence.
  • In sickle cell anemia.

9. An amino acid consists of...

  • an alpha carbon (central) bonded to an amino group (NH2), a carboxyllic group (COOH), Hydrogen atom and an R side chain.
  • alcohol
  • monomers
  • a pyramid structure

10. What is the quaternary structure of a protein?

  • protein consisting of one or more polypeptide chains. Each polypeptide chain can be a subunit and can be held together by interactions such as hydrogen bonds and disulfide bonds.
  • amino acid sequence.
  • alpha and beta pleated sheets.
  • the 3D shape.

11. Who deduced the first amino acid sequence of a protein?

  • Geremy Bennedict
  • Frederick Sanger.
  • Joseph Knucklehead
  • Jonathan Simone

12. Detail of tertiary structure can be found through...

  • Amino acid sequence.
  • Microscope.
  • X-ray crystallography.
  • Hydrogen bonds.

13. Why is the amino acid sequence of a protein important?

  • To get amino acids.
  • Because amino acid sequence determines protein structure and structure dictates biochemical function.
  • because to find Frederick Sanger.
  • oxygen.

14. What is there instead of glutamic acid in sickle cell anemia?

  • Guanine is there instead of glutamine acid.
  • Valine is present instead of glutamic acid.
  • Thymine is there instead of glutamic acid.
  • Adenine is there instead of glutamic acid.

15. Histidine is also considered...

  • a peptide bond.
  • a hydrogen.
  • polar, but can only partially charge at physiological pH.
  • nonpolar.

16. Proteins are...

  • polymers of amino acid monomers
  • gametes
  • protein synthesis
  • only in humans

17. Is it a problem if there are errors in the amino acid sequence, and what example?

  • Yes, because it will affect the oxygen.
  • No, it will not affect anything but it will cause less oxygen.
  • Yes, as this will affect the structure and then the function of the protein. For example, sickle cell anemia.
  • No. It won't affect anything.

18. What are two of the proposed polypeptide structures named by Pauling and Corey?

  • the α-pleated sheet structure, or the polar pleated sheet.
  • The amino acid.
  • The peptide bond.
  • The amino acid sequence.

19. All amino acids taken from protein (from any source) are always...

  • D- amino acids
  • L- amino acids
  • microorganisms
  • S- amino acids

20. Polypeptide chains are...

  • carbohydrates.
  • hydrogen bonds.
  • two or more amino acids joined together to form a long, continuous unbranched chain.
  • chain of carboxyl groups.