OBJECTIVES
After studying this chapter, you should be able to:
Name, and draw the structures of, the 20 amino acids present in proteins.
Write the three- and one-letter designations for each of the common amino acids.
List the ionizable groups of the common amino acids and their pKa values.
Calculate the pH of an unbuffered aqueous solution of a polyfunctional amino acid and the change in pH that occurs following the addition of a given quantity of strong
acid or alkali.
Define pI and indicate its relationship to the net charge on a polyfunctional electrolyte.
Explain how pH, pKa and pI can be used to predict the mobility of a polyelectrolyte, such as an amino acid, in a direct-current electrical field.
Describe the contribution of each type of R group of the common amino acids to their chemical properties.
Describe the directionality, nomenclature, and primary structure of peptides.
Identify the bond in a peptide that exhibits partial double-bond character and its conformational consequences in a peptide.
Identify those bonds in the peptide backbone that are capable of free rotation and the Greek letters used to designate them.
OBJECTIVESAfter studying this chapter, you should be able to:Name, and draw the structures of, the 20 amino acids present in proteins.Write the three- and one-letter designations for each of the common amino acids.List the ionizable groups of the common amino acids and their pKa values.Calculate the pH of an unbuffered aqueous solution of a polyfunctional amino acid and the change in pH that occurs following the addition of a given quantity of strongacid or alkali.Define pI and indicate its relationship to the net charge on a polyfunctional electrolyte.Explain how pH, pKa and pI can be used to predict the mobility of a polyelectrolyte, such as an amino acid, in a direct-current electrical field.Describe the contribution of each type of R group of the common amino acids to their chemical properties.Describe the directionality, nomenclature, and primary structure of peptides.Identify the bond in a peptide that exhibits partial double-bond character and its conformational consequences in a peptide.Identify those bonds in the peptide backbone that are capable of free rotation and the Greek letters used to designate them.
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