DP Biology Questionbank

Description

Nature of science:
Developments in scientific research follow improvements in computing—the use of computers has enabled scientists to make advances in bioinformatics applications such as locating genes within genomes and identifying conserved sequences. (3.7)Understandings:

• Initiation of translation involves assembly of the components that carry out the process.
• Synthesis of the polypeptide involves a repeated cycle of events.
• Disassembly of the components follows termination of translation.
• Free ribosomes synthesize proteins for use primarily within the cell.
• Bound ribosomes synthesize proteins primarily for secretion or for use in lysosomes.
• Translation can occur immediately after transcription in prokaryotes due to the absence of a nuclear membrane.
• The sequence and number of amino acids in the polypeptide is the primary structure.
• The secondary structure is the formation of alpha helices and beta pleated sheets stabilized by hydrogen bonding.
• The tertiary structure is the further folding of the polypeptide stabilized by interactions between R groups.
• The quaternary structure exists in proteins with more than one polypeptide chain.

Application and skills:

• Application: tRNA-activating enzymes illustrate enzyme–substrate specificity and the role of phosphorylation.
• Skill: Identification of polysomes in electron micrographs of prokaryotes and eukaryotes.
• Skill: The use of molecular visualization software to analyse the structure of eukaryotic ribosomes and a tRNA molecule.

Guidance:

• Names of the tRNA binding sites are expected as well as their roles.
• Examples of start and stop codons are not required.
• Polar and non-polar amino acids are relevant to the bonds formed between R groups.
• Quaternary structure may involve the binding of a prosthetic group to form a conjugated protein.

Utilization:
Syllabus and cross-curricular links:
Biology
Topic 2.7 DNA replication, transcription and translation
Option B: Biotechnology and bioinformatics

Directly related questions

• 17M.2.HL.TZ2.6b: Outline the roles of the different binding sites for tRNA on ribosomes during translation.
• 17M.1.HL.TZ2.9: Scientists have heated a solution containing the protein albumin and measured its relative alpha...
• 17M.1.HL.TZ2.11: This image is taken from a visualization of a eukaryotic ribosome. The arrows show the direction...
• 17M.1.HL.TZ1.28: Which types of interactions are found in a part of a protein with secondary but not tertiary...
• 17M.1.SL.TZ1.1: Which structure found in eukaryotes has a single membrane? A. Nucleus B. Lysosome C....
• 16N.1.HL.TZ0.28: Variations in the types of antibodies are produced by mRNA splicing. What is an advantage of this...
• 16N.1.HL.TZ0.27: What does post-transcriptional modification of eukaryotic mRNA include? I.   Introns are removed...
• 16N.1.HL.TZ0.26: Where does a tRNA-activating enzyme attach the appropriate amino acid to the tRNA molecule?
• 16M.1.HL.TZ0.8: The image represents a model of the protein transthyretin. Which level of structure is...
• 15M.3.SL.TZ2.8a: Outline primary and quaternary protein structures. Primary protein structure:   Quaternary...
• 15N.1.HL.TZ0.26: What determines the primary structure of hemoglobin? A. Genetic information B. Hydrogen...
• 15N.2.HL.TZ0.2b: State what is indicated by the presence of polysomes in a cell.
• 13N.1.HL.TZ0.27: The following diagram shows a ribosome during translation. What describes the specific stage...
• 13M.3.SL.TZ1.8a (i): Identify the level of protein structure of the part labelled X.
• 12M.2.HL.TZ1.2c (i): Label the sense and antisense strands.
• 12M.2.HL.TZ1.2c (ii): Draw an arrow on the diagram to show where the next nucleotide will be added to the growing mRNA...
• 12M.1.HL.TZ2.26: The diagram shows the cross section of a plasma membrane. What is found in area X? A....
• 12M.3.SL.TZ1.9: Explain the significance of polar and non-polar amino acids in proteins.
• 12M.3.SL.TZ2.8a: Define quaternary structure in proteins.
• 12M.3.SL.TZ2.8b: Outline the importance of polar and non-polar amino acids in proteins.
• 09M.2.HL.TZ1.1i (ii): Outline how this structure is held together.
• 09M.2.HL.TZ2.2c: Explain primary structures and tertiary structures of an enzyme.
• 09M.1.HL.TZ1.26: Which best describes the tertiary structure of a protein? A. The interaction of polypeptide...
• 09M.1.HL.TZ2.25: What is the distinction between highly repetitive DNA sequences and single-copy genes? A. The...
• 10M.2.HL.TZ1.6c: Translation occurs in living cells. Explain how translation is carried out, from the initiation...
• 10M.2.HL.TZ2.5a: Outline the structure of a ribosome.
• 17N.1.HL.TZ0.28: Which cell component synthesizes actin and myosin? A. Free ribosomes B. Rough endoplasmic...
• 17N.2.HL.TZ0.07b: Nitrogen is part of many important substances in living organisms. Distinguish between...
• 10M.2.HL.TZ2.5b: Distinguish between fibrous and globular proteins with reference to one example of each protein...
• 10M.3.SL.TZ1.10b: Explain the significance of polar and non-polar amino acids.
• 10M.3.SL.TZ2.9b: Explain the significance of polar amino acids and non-polar amino acids in membranes.
• 10M.3.SL.TZ2.9a: List three functions of proteins, giving a named example of each.
• 12N.2.HL.TZ0.7c: Outline how the structure of the ribosome is related to its function in translation.
• 12N.1.HL.TZ0.24: The diagram is a three-dimensional molecular model of a protein. Which bonds stabilize the...
• 10N.3.SL.TZ0.9: Outline the differences between these two proteins.
• 10N.2.HL.TZ0.4b: Outline the structure of ribosomes.
• 09N.2.HL.TZ0.3d: Explain the role of transfer RNA (tRNA) in the process of translation.
• 09N.3.SL.TZ0.8b: Distinguish between the secondary structure and tertiary structure of proteins.