1In a DNA double helix, what kind of chemical bonds form between the complementary nitrogenous bases?
- Nitrogen bonds
- Phosphodiester bonds
- Polar covalent bonds
- Hydrogen bonds
2What is unusual about the peptide bond compared to the other covalent bonds that form the polypeptide backbone?
- The single bonds on either side of the peptide bond cannot rotate, making the peptide backbone very rigid.
- There is an amino group on one end of the backbone and an aldehyde group on the other.
- Peptide bonds behave like double bonds in terms of stability and lack of movement of atoms around the bond.
- The side chains only face internally, excluding them from interacting with water.
3The condensation reaction that forms nucleic acid polymers occurs between a _____ group on one nucleotide and a _____ group on a second nucleotide.
Phosphate; Hydroxyl
4What type of bond is directly involved in the formation of anα-helix?
- Peptide bonds between amino acid residues
- Van der Waals interactions between nonpolar residues
- Hydrogen bonds between amino acid residues
- Disulfide bonds between cysteine residues
5What determines the primary structure of a DNA molecule?
Deoxyribonucleotide Sequence
6Which of the following statements about protein primary structure is true?
- Primary structure is maintained through hydrogen bonds.
- Primary structure results when two or more protein molecules interact with each other.
- Primary structure is produced when a protein is chemically modified.
- Primary structure is produced by the unique sequence of amino acids in a protein.
- Primary structure comes about through interactions between the side chains on different amino acids.
7Which of the following parts of an amino acid vary among different amino acids?
- The phosphate group
- The carboxyl group
- The hydrogen on the central carbon
- The amino group
- The side chain, or R group
8All of the following are examples of protein functions except one. Identify the exception.
- Catalysis
- Transport
- Self-replication
- Defense
- Signaling
9Explain how molecular chaperones facilitate protein folding in many different polypeptides, each with their own specific shape.
- by preventing unfolded proteins from clumping together
- by treating it with compounds that break hydrogen bonds and disulfide bonds
- by binding substrates at their active site, where catalysis takes place
- by changing the primary structure of improperly folded proteins
10Which tupes of R-groups easily dissolve in water
11Which types of R-groups do not interact with water?
12A small organic molecule with a central carbon atom that is the building block for proteins
Amino Acids
13Part of an amino acid's core structure that caries from a single hydrogen atom to large structures containing carbon rings.
R-group
14The two types of covalent bonds:
Polar and Non-Polar