a-subunit of human hemoglobin Bacteriorhodopsin Below are amino acid sequences.of the E-helix of the a-subunit of human hemoglobin and of helix-4 of Halobacterium bacteriorhodopsin. With the aid of the helical wheels on the next page, decide which helix belongs to the a-subunit of hemoglobin and which belongs to bacteriorhodopsin. Upon identifying which amino acid sequence belongs to which protein, explain how the differences in amino acid com- position and sequence reflect the environment of each protein. 10 20 | Helix 1 GTILALVGANGIMIGTGLVGALT Helix 2: SAQVKGHGKKVADALTNAVA

(A) Give the polypeptide translation of the RNA sequence below. 5’-AUGGAAAUCAAAGUCAACCUUGAGUUUAGA-3’ (B) Write the chemical structure of the polypeptide sequence you determined in part (a) (C) Given the chemical structure of the polypeptide sequence you have written in part (b), answer True or False for each of the 5 statements below. (1) At least one of the amino acids in the sequence can undergo phosphorylation (2) The sequence looks like it could form a β turn (3) The sequence looks like it could form a β strand with one surface facing the interior of the protein and the other surface exposed to water (4) At least one of the amino acids in the polypeptide sequence can undergo oxidation to form a disulfide bridge to another polypeptide (5) The sequence looks like it could form an α helix that would be part of a coiled coil structure within a protein

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A protein of unknown structure has been purified. Size-exclusion chromatography reveals that the native protein has a MW of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields a single peak corresponding to a protein of MW 60,000. Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM B-mercaptoethanol yields peaks for proteins of MW 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data.