I have made a lineweaver-burk graph with some data, but I don't know how to determine Vmax and Km from it? Would you please give me an example of how to do it. Please make a lineweaver-graph with some values and tell me how to determine Km and Vmax. I can figure out the slope from the graph, but cannot figure out Y and x in Y
Which fatty acid -palmitic, stearic, palmitoleic, or arachidonic, would have lowest m.p. and explain why. Which would be chiral? A)glyceryl tripalmitate,B) glyceryl 1-stearate, 2,3 dipalmitate,C) glyceryl 2-stearate, 1,3-dipalmitate. Explain why. A lipid is isolated and treated with boiling aqueous NaOH. The products ob
Dear OTA, I have 2 multiple questions as attached. I have done those but have some doubts. The questions are in red and my answer is in black. Need to get explanation why the option B in #61 is wrong (heavy references) and why option A in #53 is wrong (also references) Basically I need to know why only 1 option is good for
Question #1: (1 point) In the urea cycle, the molecule that is synthesized in the cytosol and transported to the mitochondrial matrix for subsequent reactions is a.) citrulline b.) ornithine c.) argininosuccinate d.) aspartate e.) carbamoyl-phosphate Question #2: (1 point) Inosine 5'-phosphate is a precursor to which
A two electron transfer reaction you are studying has a standard state standard reduction potential (Eo') on 0.137V at 37C.
A two electron transfer reaction you are studying has a standard state standard reduction potential (Eo') on 0.137V at 37C. What is the equilibrium constant for the reaction (Keq') at 37C?
Guanyl nucleotide regulatory proteins (N) alter cell function based on the type of guanyl nucleotide occupying the nucleotide site on the protein. The affinity of this site for guanyl nucleotides is to a certain extent under hormonal control. Given a Ka of the site for guanyl nucleotides of 3 x 10^7 M in the presence of hormon
1 BCH-100 Fall 2007 BLH #13 (4 points) Question #1: (0.8 point) How many acetyl CoA's will come from a 12 carbon acyl-CoA? a.) 5 b.) 6 c.) 7 d.) 12 e.) none Question #2: (0.8 point) How many acetyl CoA's will come from a 13 carbon acyl-CoA? a.) 5 b.) 6 c.) 7 d.) 12 e.) none Question #3: (0.8 point) How many p
Lineweaver-Burk Plot from Absorbance Data (with and without inhibitor) and Michaelis-Menten Kinetics
I carried out a practical last week and need to write it up but canot remember how to do the calculations from the Michaelis-Menten graph plotted which I guess helps me to plot a Lineweaver-Burk. I have attached the practical requirements. I have to produce a table (attached) but cannot fill in certain columns until I can work
Why are most of the fatty acids found in animal tissues composed of an even number of carbon atoms?
Fumarase deficiency is an extremely rare disease in humans. People with this disease can survive although they are significantly affected. a) Given the importance of fumarase to the citric acid cycle how is it possible for people with fumarase deficiency to produce adequate ATP for survival? b) what would be the overall
Please see attached file.
Part 1: what is equilibrium concentrations and concentration ratios of glucose-6-phosphate/glucose-1-phosphate in the phosphoglucomutase reaction when the initial concentration of glucose-6-phosphate is (a) .01 M and (b) 10^-3 M. The Keq for the reaction below is 19. Glucose-1-phosphate ---> glucose-6-phosphate Part 2: wh
Fructose-1,6-diphosphate can be converted to glucose-1-phosphate by three successive reactions: Fructose 1,6 diphosphate + H20 ---> fructose-6-phosphate + Pi Keq= 607 Fructose-6-phosphate ---> glucose-6-phosphate G°= -410 cal/mol Glucose-6-phosphate --->glucose-1-phosphate G°= 1750 cal/mol As
Non-competitive inhibitors of enzymes change the slope and Km of a Lineweaver Burk graph compared to no inhibitor. a.) True b.) False
You want to make a 0.1M acetate buffer from 0.1M solutions of acetic acid and acetate. How many mL of acetic acid would you need per liter of solution (with the rest of the volume coming from the acetate solution) to generate a pH of 4.75? The pKa of acetic acid is 4.76
The pKA of histidine in a protein active site where it is next to an aspartate or glutamate would be____________ the pKa of free histidine solution higher, lower, no different Is it higher??
For the hydrolysis of phosphocreatine: Phosphocreatine + H2O==creatine + Pi the standard state deltaG is -42.8 kJ/mol at 37 degrees celsius. If in a given cell the concentration of creatine is 1.7mM, phosphate is 5.8mM, and phosphocreatine is 6.4mM, what is the deltaG for hydrolysis of phosphocreatine in the cell? Nearest 0.
The equilibrium constant for the denaturation of a protein is determined to be 0.13 at 59.8 degrees Celsius. What is the standard state of delta G for the reaction, in kJ/mol to 0.01kJ/mol.
The phosphate system serves to buffer the intracellular fluid of cells at physiological pH because pK2 (7.20) lies near the normal pH range of 6.9-7.4. If the total cellular concentration of phosphate is 19mM and the pH is 6.9, what is the concentration of (H2PO4-) in mM?? Is this correct??? H2PO4-(aq) H+(aq) + HPO42-(aq)
What affect does the presence of metal ions like Mg++ in the cell have on free energy of hydrolysis of ATP?? raise, lower, or no affect why??
The following questions refer to the mitochondrial enzyme MALATE DEHYDROGENASE. What is the chemical reaction, within the citric acid cycle, that is catalyzed by malate dehydrogenase, and which substrates, products, and/or cofactors are involved? The reaction from the previous question is classified as a dehydrogenatio
Lactate dehydrogenase catalyzes the reversible reaction: Pyruvate + NADH + H^(+) --> Lactate + NAD^(+) Given the following facts, (a) tell in which direction the reaction will tend to go if NAD^(+), NADH, pyruvate, and lactate were mixed, all at 1 M concentrations, in the presence of lactate dehydrogenase at pH 7; (b) calc
See attached file for full problem description. Which structures contain saturated fatty acids or saturated fatty acid derivatives? Select all answers that apply. a. A b. B c. C d. D e. E Which structures contain unsaturated fatty acids or unsaturated fatty acid derivatives? Select all an
Provide the complete & accurate systematic name for this molecule. Be sure to include the correct names, in order, of the sugar residues, the correct numeric linkage for the glycosidic bonds, and any necessary information about anomeric carbons. See attached file for trisaccharide molecular formula. The first monosacchari
If the following peptide was the substrate for Carboxypeptidase A. Which of the indicated red arrows correctly identifies the scissile bond? See attached file for full problem description.
1) Carboxypeptidase A, a zinc-containing enzyme, hydrolyzes the C- terminal peptide bonds of polypeptides and/or proteins. In the enzyme- substrate complex, the zinc ion is coordinated to three enzyme side chains, the carbonyl oxygen of the scissile peptide bond, and a water molecule. A plausible model for the enzyme's reaction
Step-by-step explanation of how to calculate the pKa of a weak acid of known pH and concentration.
I have followed the procedure that you provided to determine the activity of the beta glucosidase, however what I am unsure of is how the rate is calculated? In order for me to establish the rate, I followed your instructions however incubated the enzyme/buffer and PNPG solution for different times, ranging from 0-16 minut
Make the following dilution: a working concentration of 100 ml 15 U/uL from an enzyme stock of 756,431 U/uL. Will you use a serial dilution? Why or Why not?
Describe the effects the following would have on the way you PAGE gel would run: a) Increasing the percent of acrylamide b) Increasing the pH of the Tris-glycine buffer to 9.5 c) Decreasing the voltage at which the gel was run d) Increasing the voltage at which the gel was run by a factor of 3 e) Doubling the sample load vo