A protein contains four arginyl, residues and sis, lysyl residues. However, in i

Question

A protein contains four arginyl, residues and sis, lysyl residues. However, in its native state a protease digest with trypsin only yields 4 fragments. 0 1 2 3 4 What does this tell you about the structure of the protein? its dynamic, with great deals of movement Globular structure Elongated structure No information can be learned What interactions are the majority of the side chains of arginyl and lysyl residues most likely part of? Covalent bonds Disulfide bonds Peptide bonds Hydropbobic interactions Ionic bonds bonds bonds interactions A protein has an active site tunnel lined with the aromatic residues Tyr and Phe. It is believed that the substrate binds to the active site tunnel through hydrogen bonding Interactions. To determine if this is the case, you decide to make mutations within the active site with the goals of disrupting hydrogen bonds between protein and substrate and to minimally affect the structure of the protein. Which of the following mutations do you make in the active site? Mutate all Tyr to Phe Mutate all Phe to Tyr Mutate all aromatics to Trp Mutate all Tyr to Ala Mutate all Phe to Trp A protein has a pl of 9. What conclusion can be made about the types of residues likely comprising this protein? Most likely to have numerous residues with positively charged side chains Most likely to have numerous residues with negatively charged side chains Most likely to have numerous residues with polar uncharged side chains a and c b and c With a protein with a pl of 9, which type of chromatography are you most likely to use for purification based on that information? Gel filtration SDS-Gel Electrophoresis Anion exchange Cation exchange Hydrophobic interaction

Explanation / Answer

7. (D) The four fragments are obtained by cleavage of 3 peptide bonds by trypsin.

8. (B) Such protein may have a globular structure.

9. (C) Peptide bonds

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