Both α-keratin and tropocollagen have helical secondary structure. How do these molecules differ in (a) amino acid composition and (b) three-dimensional structure?
If the same peptide found in Problem 18.32 is subjected to acid hydrolysis, how many fragments will result? Why?
Ala-Phe-Lys-Cys-Gly-Asp-Arg-Leu-Leu-Phe-Gly-Ala
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Key Concepts
Acid Hydrolysis
Peptide Structure
Fragmentation Analysis
Draw the structure of the following amino acids, dipeptides, and tripeptides at low pH (pH 1) and high pH (pH 14). At each pH, assume that all functional groups that might do so are ionized.
a. Val
Another endoprotease is trypsin. Trypsin hydrolyzes peptide bonds on the carboxyl side of lysine and arginine. If the following peptide sequence is hydrolyzed by trypsin, how many fragments will there be? Use the three-letter amino acid abbreviations to write the fragments out.
Ala-Phe-Lys-Cys-Gly-Asp-Arg-Leu-Leu-Phe-Gly-Ala
Draw the structure of the following amino acids, dipeptides, and tripeptides at low pH (pH 1) and high pH (pH 14). At each pH, assume that all functional groups that might do so are ionized.
e. Gln-Ala-Asn
For each of the conjugated proteins described, identify to which class of conjugated protein it belongs.
c. Phosphate groups are attached to this protein.
Draw the structure of the following amino acids, dipeptides, and tripeptides at low pH (pH 1) and high pH (pH 14). At each pH, assume that all functional groups that might do so are ionized.
d. Glu-Asp
