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Unformatted text preview: .5 5.9 7.3 7.9 8.1 Use the Lineweaver‐Burk plot to determine the values of Km and Vmax of the enzyme in the absence of inhibitors. Express your Km and Vmax values in µM and µmol min‐1, respectively. On the same graph determine the apparent Km and Vmax values (in µM and µmol min‐1) of the enzyme in the presence of inhibitor Y. What type of reversible inhibitor is Y? Explain your answer. Tutorial 1 Questions Page 1 of 3 LSM1401 3. 4. Semester 2 2008‐09 The pKa values of the α‐carboxyl, side chain, and α‐amino groups of aspartic acid are 1.88, 3.65, and 9.60, respectively. (a) Draw the predominant form of aspartic acid at pH 7. 注意是protonated 还是de-protonated (b) What percentage of the side chain group is deprotonated at pH 4? (c)
A researcher was able to modify the aspartic acid by replacing the hydrogen that is attached to the α‐carbon with another amino group. (i)
Draw the structure of the new amino acid when its net charge is zero. (ii)
Calculate the isoelectric point for this new amino acid. Assume that the pKa for the new...
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This note was uploaded on 10/11/2012 for the course BIOLOGY 1401 taught by Professor Siewteckkeong during the Spring '12 term at National University of Singapore.
- Spring '12