Calculate the mass of disodium EDTA (FW 372.25) needed to make 500-mL 0.015 M solution of EDTA. What is the equilibrium concentration of Y4- if the pH is (1) 7.00, and (2) 9.00?
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Calculate the mass of disodium EDTA (FW 372.25) needed to make 500-mL 0.015 M solution of EDTA. What is the equilibrium concentration of Y4- if the pH is (1) 7.00, and (2) 9.00?
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- When we perform Bradford Assay to measure protein concentration, the spectrophotometer is set 595 nm because: a. the excitation peak of Coomassie Blue is best observed at 595 nm b. when Coomassie Blue binds to proteins, its maximum absorbance shifts to 595 nm c. the reducing effects of Coomassie Blue shifts the protein's maximum absorbance to 595 nm d. myoglobin is best observed at 595 nmWhy is it reasonable that the Ksp of NiCl2 should be so high? given: NiCl2~~>Ni2+(aq)+2Cl-(aq) ksp=497.504 ksp=[Ni2+][Cl-]^2 [Ni2+]=4.992 [Cl-]=9.983The catalytic activity of an insect aminopeptidase was investigatedusing an artificial peptide substrate. The Vmax was 4.0 × 10-7 M/s and the KM was 1.4 × 10-4 M. The enzyme concentration used in the assay was 1.0 × 10-7 M. What is the value of kcat? 2.86 x 10-3 M 0.25 M/s 4.0 s-1 2.86 x 104 s/M 0.25 s-1
- Could someone explain what this is saying? I would like a better understanding. FIGURE D CPP32 (Caspase-3) protease activity. Aliquots of cell lysates (50μL) were incubated with an equal volume (50 μL) of the reactionbuffer and 5 μL of 7-amino-4-trifluoromethyl coumarin (AFCDEVD) for 1 hour at 37˚C (Clontech). The shift in fluorescenceemission of AFC-DEVD, on its proteolysis to free AFC by theprotease, was detected in a fluorometer, using a 400 nm excitationfilter and 505 nm emission filter.Please determine Hvap using these: P2- 3.7kpaP1- 19.2kpa T2-276.65KT1-330.15Kwhat is the concentration of the unknown sample using serial diluitions: 0.05M 1.7472nm, 0.025M 0.8569nm, 0.0125M 0.4167nm, 0.00625M 0.1958nm the epsilon value is 0.0101 and l is 1 cm
- Based on the chemical reactions provided, which of the following is equivalent to KCa-EDTA? a. [Ca2+] [EDTA2-] b. [Ca-EDTA] / {[Ca2+] [EDTA2-]} c. {[Ca2+] [EDTA2-]} / [Ca-EDTA] d. {[Ca-EDTA][Ind2-]} / {Ca-Ind] [EDTA2-]}Which is incorrect regarding ligand-protein binding reactions? Select one: Allosteric modulation can alter the affinity of the protein for the ligand. Phosphorylation of the protein is an example of covalent modulation. Allosteric modulation of the protein’s binding site occurs directly at the binding site itself. If two ligands can bind to the binding site of the protein, competition for binding will occur. Binding reactions are either electrical or hydrophobic in nature.Calculate the (a) Linearity constant (r), (b) y-intercept, (c) Slope, and (d) Protein content of an unknown sample having an absorbance of 0.325.
- INORGANIC Chemistry Starting product was [(Me5dien)CoCl2] and reacted with NaSCN to produce [(Me5dien)Co(SCN)2] Using the graphs attached, the IR data tells you that the binding mode is N coordination. How does the IR data agree (or disagree) with the peak shifts (Uv-Vis spect) IR Product 1, [(Me5dien)CoCl2] 29041.04, 2812.76, 2761.62 cm-1 (carbon bond) 1457.35 cm-1 (CH2) 1263.91 cm-1 (possibly C-N stretch) Product 2, [(Me5dien)Co(SCN)2] 2968.54-2870.67 cm-1 (C-C) 2059.41 cm-1 (N=C=S) 1470.28 cm-1 (CH2) Uv-vis [(Me5dien)CoCl2] Peak A: 531.8 nm, 0.722 Abs Peak B: 609.7 nm, 0.666 Abs [(Me5dien)Co(SCN)2] Peak A: 510.20 nm, 0.357 Abs Peak B: 608.20 nm, 0.401 AbsUsing the following data to calculate Ksp for PbSO4. ε° PbO2 + 4H+ + SO42- + 2e-→ PbSO4(s) + 2H2O +1.69 PbO2 + 4H+ + 2e-→ Pb2+ + 2H2O +1.46 (Hint: Write the general reaction for PbSO4) a. 1.7 × 10-8 b. 5.9 × 107 c. 2.5 × 10-107 d. 4.0 × 10106 e. 3.4 × 10-18A sample of adenosine triphosphate (ATP) (MW 507, e 5 14,700 M-1cm-1 at 257 nm) is dissolved in 5.0 mL of buffer. A 250-mL aliquot is removed and placed in a 1 cm cuvette with sufficient buffer to give a total volume of 2.0 mL. The absorbance of the sample at 257 nm is 1.15. Calculate the weight of ATP in the original 5.0 mL sample.