# Q1. Standard curve. In a full-credit answer, standard curve plo...

## Question

Q1. Standard curve.

In a full-credit answer, standard curve plot has the correct x- and y­axes (not inverted); axes are labeled and include units.

Graph contains a trendline, but this does not obscure the individual data points.

A calculated R-squared value is present on the graph.

A paragraph clearly describes the graph (axes? units? tested range? linearity or lack thereof?), mentions the actual color of the tested solution, and comments on the R-squared value and any factors in the lab that may have led to deviations from a 1.0 value.

Q2. Michaelis-Menten data.

In a full-credit answer, table includes all required data and correctly uses the standard curve to generate Vo data.

Michaelis-Menten plot has the correct x- and y-axis (not inverted); axes are labeled and include units.

A paragraph clearly describes the graph (axes? units? tested range? enzyme concentration? linearity or lack thereof? comparison with expected shape?), and provides an estimated numerical Km, Vmax, and kcat (including units and an appropriate number of significant digits).

It is clear how the Km and Vmax estimates were obtained, and how the kcat was subsequently calculated.

Q3. Lineweaver-Burk plot.

A full-credit answer has a table that includes all required data and clearly through column headers and units indicates that these values are reciprocals.

Lineweaver-Burk plot has the correct x- and y-axes (not inverted); axes are labeled and include units.

A paragraph clearly describes the graph (axes? units? relationship to previous graph? linearity or lack thereof? comparison with expected shape?), and provides an estimated numerical Km, Vmax, and kcat (including units and an appropriate number of significant digits).

It is clear how the Km and Vmax estimates were obtained, and how the kcat was subsequently calculated:

Q4. Alkaline phosphatase active site figures.

A full-credit answer contains two figures.

The first one shows the AP active site residues surrounding the inorganic ions, and the caption is extremely thorough and in complete sentences (visualization program, filename, resolution, structure determination method, name of organism, name of protein, multimeric status, chain length, inorganic ions in view and obscured from view, active site residues in view and obscured from view, lab partner if applicable).

Should also identify likely electrostatic attractions in the active site and their likely significance.

The second figure should show a translucent surface view of the same active site, and be captioned as such, giving the style and color used.

Q5. Alkaline phosphatase mutagenesis experiments.

In a full-credit answer, two clear and detailed paragraphs are provided.

The first discusses the mutagenesis data, drawing a clear conclusion about which residue appears to play the role of attacker, and whv the other residues in the mutagenesis experiment can be ruled out.

The second paragraph uses information from the PDB website to identify an additional residue (not part of the Jmol activity) that appears to function in metal binding.

Its R-group chemistry is described, including expected charge at the operating pH of alkaline phosphatase.

A new experiment in which this residue is mutated to an alternate amino acid is proposed, and the rationale for choosing the new amino acid is clearly explained.

Q6. Alkaline phosphatase inhibition data analysis.

In a full-credit answer, two clear and detailed paragraphs are provided.

Both are comparable in content, except that the first discusses the first inhibition graph that was provided, and the second discusses the second inhibition graph that was provided.

Each paragraph includes the chemical name of the inhibitor, the effect that the chemical had on the slope and/or y-intercept of the L-B plot, an explicit conclusion that the inhibitor is competitive/uncompetitive/noncompetitive and an explanation of what distinguishes that type of reversible inhibitor from the other two, a statement regarding whether the conclusion regarding inhibitor type could have heen made as readily if the data had heen plotted on a standard Michaelis-Menten plot, and a prediction (as specific as possible) regarding where the inhibitor would be likely to bind.

For the second paragraph, a statement should also speculate on why inorganic phosphate would serve as an inhibitor at all.

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