BCH 403 Final Exam questions with complete solutions
You're using anion exchange chromatography to purify a small globular protein. After passing the mixture through the column, you find that your protein did not "stick" to the resin and flowed right through. What is a plausible reason for this to have occurred? Correct Answer-The pH of the solution is close to the isoelectric point. Oxygen binding that affects the cooperatively of hemoglobin is an example of heterotrophic regulation. Correct Answer-False You have determined that a leucine amino acid residue is important for the function of a bacterial protein. You suspect that the size and the nonpolar nature of leucine has something to do with it. You decide to test this idea by mutating the residue into a different amino acid. Which of the following replacements would give you the most similar data to the natural protein? Correct Answer-Isoleucine Which of the following is NOT involved in the cooperativity of Hemoglobin (Hb)? Correct Answer-The tetramer will temporarily have two binding sites in the Oxy state, and two binding sites will be in the Deoxy state. The following protein sequence is composed mostly of right-handed alpha-helices.
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