Amino acid charges at various pH

Can someone check my answers to the following, please make any corrections and explanations as needed.... N---Tyr---Lys---Thr---C pka 9.1 10.1 10.5 13 2.6 ph2 +1 0 +1 0 0 =+2 ph6 +1 0 +1 0 -1 =+1 ph13 0 -1 0 0 -1 =-2 N---Asp---Met---Ala---C ...continues

Question on Enzymes

This is a question on enzymes for a report - can't seem to come up with an answer. What are the basic units of enzymes and how are these units arranged and under what conditions do enzymes work best? Thanks for your help!!!

Plotting a titration curve for Ala and His

- calculate as many points on the curve as needed to discern its basic charcteristics. - state any assumptions you have made - plot points on a graph (simple excel graph is perfect): be sure calulcated point are visible with the curve (especially at inflection and equilibrium of the sigmoid, etc) - general commens on what is ...continues

Finding the primary structure of an unknown peptide

2. The following results were obtained for an unknown peptide in an effort to deduce the primary structure. The N-acetyl and N-formyl groups indicated in the data below would be cleaved from their respective residues during acid hydrolysis -assume that additional procedures have determined their linkages. Determine the primary s ...continues

Biochem Structures- enzyme inhibitor in a reaction (comp. or non-comp?)

This is an enzyme inhibitor problem which includes a quick plotting of a curve. it is the intro problem to a set of like examples I am working through. This is the easiest of that set. I am hoping to use your work on this to apply to the more complex examples. Explanations of steps and clear calculations would be very help ...continues

Biochem- KM of a Michaelis-Menten enzyme

5. The KM of a Michaelis-Menten enzyme for a substrate is 1.0 x 10-4 M. At a substrate concentration of 0.2 M, νo = 43 μM x min-1 for a certain enzyme concentration. However, with a substrate concentration of 0.02 M, νo has the same value. (A) Using numerical calculations show that this observation is accurate. ...continues

How to Calculate Vmax and Km from Enzyme Activity Data using a Lineweaver-Burk Plot

The activity of an enzyme was determined in the presence and absence of a suspected inhibitor. You can see the activity data in the attached Word document. Plot the data using the double reciprocal plot (Lineweaver-Burk) to determine whether the suspected inhibitor acts noncompetitively, competitively, or uncompetitively. Cal ...continues

Michaelis-Menton eq

(See attached file for full problem description) --- 1. For a Michaelis-Menten reaction, k1 = 5 x 107 M-1 s-1, k-1 = 2 x 104 s-1, and k2 = 4 x 102 s-1. Calculate Ks and Km for this reaction. Does substrate binding achieve equilibrium or the steady state? 2. At what substrate concentration will an enzyme having a kcat of ...continues

Enzyme

(See attached file for full problem description with proper symbols and equations) --- 2. Carbonic anhydrase of erythrocytes (Mr 30,000) is among the most active of know enzymes. It catalyzes the reversible hydration of CO2: H2O + CO2 H2CO3 which is important in the transport of CO2 from the tissues to the lungs. If ...continues

LADH PROBLEM

1. Ethanol in the body is oxidized to acetaldehyde by liver alcohol dehydrogenase (LADH). Other alcohols are also oxidized by LADH. For example, methanol, which is mildly intoxicating, is oxidized by LADH to the quite toxic product formaldehyde. The toxic effects of ingesting methanol (a component of many commercial solvents) ...continues