Chapter 27: Problem 41
If a protein contains four different SH groups, how many different disulfide bonds are possible if only a single disulfide bond is formed? How many different disulfides are possible if two disulfide bonds are formed?
Chapter 27: Problem 41
If a protein contains four different SH groups, how many different disulfide bonds are possible if only a single disulfide bond is formed? How many different disulfides are possible if two disulfide bonds are formed?
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Get started for freeDraw zwitterion forms of these amino acids. (a) Valine (b) Phenylalanine (c) Glutamine
Draw a structural formula for Lys-Phe-Ala. Label the \(N\)-terminal amino acid and the C-terminal amino acid. What is the net charge on this tripeptide at \(\mathrm{pH} 6.0\) ?
Many plasma proteins found in an aqueous environment are globular in shape. Which amino acid side chains would you expect to find on the surface of a globular protein and in contact with the aqueous environment? Which would you expect to find inside, shielded from the aqueous environment? Explain. (a) Leu (b) Arg (c) Ser (d) Lys (e) Phe
Write the zwitterion form of alanine and show its reaction with the following. (a) \(1 \mathrm{~mol} \mathrm{NaOH}\) (b) \(1 \mathrm{~mol} \mathrm{HCl}\)
The side-chain carboxyl groups of aspartic acid and glutamic acid are often protected as benzyl esters. (a) Show how to convert the side-chain carboxyl group to a benzyl ester using benzyl chloride as a source of the benzyl group. (b) How do you deprotect the side-chain carboxyl under mild conditions without removing the \(B O C\)-protecting group at the same time?
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