The R groups of the residues in a peptide chain alternate on

The R groups of the residues in a peptide chain alternate on either side of the chain and are said to be in configuration. If they were in the _____configuration, they would likely clash and destabilize the structure. According the accepted convention, the directionality of a polypeptide is always from the _____ terminal to the _____ terminal. Aspartate and glutamate are where as arginine and lysine are m amino acids. Aspartame is a _____ whereas glutathione is a _____ You have just made a solution by combining 50 mL of a 0.1 M sodium acetate solution with 150 mL of 1 M acetic acid (pKa = 4.7). What is the pH of the resulting solution? How many grams of solid NaOH (m, w, 40) are required to prepare 200-mL of a 0.05 M solution? How many milliliters of 5 M NaCI are required to prepare 1500mL of0.002 M NaCl? For a weak acid with a pK_a, of 6.0, show how you would calculate the ratio of acid to base at pH 5. What are the structural characteristics common to all amino acids found in naturally occurring proteins? Give the general Henderson-Hasselbalch equation and sketch the plot it describes (pH against amount of NaOH added to a weak acid). On your curve, label the pKa for the weak acid and indicate the region in which the buffering capacity of die system is greatest.

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Q7. Trans and Cis

Q8. N- terminal (Amino) to the C- terminal (corboxyl terminal)

Q9. Acidic and Basic

Q10. Dipeptide (L-Aspartyl-L-phenylalanine methyl ester) where as glutathione is Tripeptide (gamma-glutamyl-cysteinyl-Glycine)