Chapter 6: Q5CP (page 145)
Count the number of α helices and β sheets in carboxypeptidase A (Fig. 6-12).
Short Answer
Carboxypeptidase A in the figure consists of 8 α helices and 8 β sheets.
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Chapter 6: Q5CP (page 145)
Count the number of α helices and β sheets in carboxypeptidase A (Fig. 6-12).
Carboxypeptidase A in the figure consists of 8 α helices and 8 β sheets.
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Helices can be described by the notation , where is the number of residues per helical turn and is the number of atoms, including , in the ring that is closed by the hydrogen bond.
(a) What is this notation for the helix?
(b) Is the helix steeper or shallower than the helix?
(a) Is Trp or Gln more likely to be on a protein’s surface? (b) Is Ser or Val less likely to be in a protein’s interior? (c) Is Leu or Ile less likely to be found in a middle of an α helix? (d) Is Cys or Ser more likely to be in a β sheet?
In prokaryotes, the error rate in protein synthesis may be as high as 5 × 10−4 per codon. What fraction of polypeptides containing (a) 500 residues or (b) 2000 residues would you expect to contain at least one amino acid substitution?
The genetically engineered proteins that accumulate in bacterial inclusion bodies (Fig. 5-2) form amyloid structures. Such proteins are often difficult to recover in functional form from the bacteria. Explain.
Summarize the types of information provided in a PDB file.
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