Essential Idea:   Information transferred from DNA to mRNA is translated into an amino acid sequence.
  • Outline answer to each objective statement for topic 7.3 (coming soon)
  • Quizlet study set for this topic (coming soon)
At SHS, Topic 7.3 is taught in the following class unit(s):​​​​​​​​​
7.3.U1  Initiation of translation involves assembly of the components that carry out the process.
  • Outline the process of translation initiation.
7.3.U2  Synthesis of the polypeptide involves a repeated cycle of events.
  • Outline the process of translation elongation, including codon recognition, bond formation and translocation.
  • State the direction of movement of the ribosome along the mRNA molecule.
7.3.U3  Disassembly of the components follows termination of translation.
  • Outline the process of translation termination, including the role of the stop codon.
7.3.U4  Free ribosomes synthesize proteins primarily for secretion or use in lysosomes.
  • State the difference between free and bound ribosomes.
  • List destinations of proteins synthesized on free ribosomes.
7.3.U5  Bound ribosomes synthesize proteins for use primarily within the cell.
  • List destinations of proteins synthesized on bound ribosomes.
  • Outline how a ribosome becomes bound to the endoplasmic reticulum.
7.3.U6  Translation can occur immediately after transcription in prokaryotes due to the absence of a nuclear membrane.
  • Compare the timing and location of transcription and translation between prokaryotes and eukaryotes.​
7.3.U7  The sequence and number of amino acids in the polypeptide is the primary structure.
  • Describe the primary structure of a protein, including the type of bonding involved.
7.3.U8  The secondary structure is the formation of alpha helices and beta pleated sheets stabilized by hydrogen bonding.
  • Describe the secondary structure of a protein, including the type of bonding involved.
  • Identify the alpha-helix and beta-pleated sheet in images of protein structure.
 7.3.U9  The tertiary structure is the further folding of the polypeptide stabilized by interactions between R groups.
  • Describe the tertiary structure of a protein, including the types of R group interactions involved.
  • Explain how the chemical characteristics of R groups in the polypeptide chain affect protein folding.
7.3.U10  The quaternary structure exists in proteins with more than one polypeptide chain.
  • Outline the quaternary structure of protein folding.
  • Describe the structure of a conjugated protein, including the  prosthetic group.
7.3.A1  tRNA-activating enzymes illustrate enzyme-substrate specificity and the role of phosphorylation.
  • State the role of the tRNA activating enzymes.
  • Outline the process of attaching an amino acid to tRNA by the tRNA activating enzyme.
7.3.S1  The use of molecular visualization software to analyze the structure of eukaryotic ribosomes and tRNA molecules.
  • Describe the structure of the ribosomes, including the small and large subunits and the names and roles of the tRNA binding sites.
  • Use molecular visualization software to view and identify the small and large subunit and tRNA binding sites of the ribosome.
  • Outline the structure of tRNA molecules.
  • Use molecular visualization software to view and identify the anticodon and amino acid binding site of a tRNA.
7.3.S2  Identification of polysomes in electron micrographs of prokaryotes and eukaryotes.
  • Outline the structure of a polysome.
  • Identify the beginning of an mRNA strand in a micrograph of polysomes.
7.3.NOS  Developments in scientific research follow improvements in computing- the use of commuters has enabled scientists to make advances in bioinformatics applications such as locating genes within genomes and identifying conserved sequences.
  • Define bioinformatics.
  • Outline why computers are necessary for genome analysis.
  • List seven species for which the entire genome has been sequenced.  
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