Dr. Terry L. Helser, Professor of Chemistry
227 Physical Sciences Building, Oneonta, NY 13820-4015
Phone: (607)436-3518 or Email to: HELSERTL@oneonta.edu.
Study Guide - Biochemistry, The Molecular Basis of Life, 4th Ed.,
2009, T. & J.R. McKee (Oxford Univ. Press)
Chapter 19: Protein Synthesis
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section or gene expression
How do we know that the result of gene expression is specific proteins?
1909 Archibald ______ published "Inborn Errors of Metabolism"
1940 ______ and _____ produced auxotrophic (define?) mutants
in Neurospora crassa
- Studied Alkaptonuria (urine color? _____ ) and _______________ (PKU),
- Proposed these genetic diseases were caused by the lack of _______
(not even known to be proteins at that time).
- Couldn't test this idea in humans. Why not?
The gene and its product are said to be collinear. What does this
mean? Theoretically, how many bases are needed in a sequence to specify
the 20 genetically determined (that is, genecoded) amino acids?
How was this proven and then solved?
How many codons specify amino acids?
What codons have no tRNA with anticodons specific for them?
What is their function? Note table 19.1
- linked to specific enzyme defect in each case = One ____ / One ______
- How must this be modified to fit current definitions of a "gene" and
The genetic code is degenerate and universal.
What type of code may have been the evolutionary precursor to
the current triplet code?
The code is mutationally conservative.
Which positions can suffer single base changes that produce silent
Which produce chemically similar amino acid substitutions (missense
Which usually produce nonconservative substitutions?
What are the steps in prokaryotic translation?
Where is the activation energy used?
Which RNAs are involved and how?
Which subunits, or does the whole ribosome, participate in each step?
Where does translation (the specific recognition
of an amino acid by a nucleic acid sequence) actually occur?
Why is this reaction as accurate as it is?
In which direction is the mRNA translated?
In which direction is the protein synthesized, etc.?
What is the start signal in E.
coli? ...in eukaryotes?
What are the A and P sites of the
How does EF-Tu function during aminoacyl-tRNA
binding to the A site? (See Box 19.1)
What is peptidyl transferase? In
which step(s) does it function?
Where do translocation and post-translational
modification occur? What is the folding problem? (See p. 692ff and Special
Interest Box 19.2)
What is the stop signal(s)?
How do missense, nonsense and frameshift mutations relate to translation
and the genetic code?
In chapter questions 19.1-3, 19.4-6,
End of chapter review questions: 1.-9.,
13., 14., 17., 18. Thought Questions: 1.-14.
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Last Modified on 7/16/2008