(Please draw) Illustrate the intermolecular forces expected to be found in an oil-water interface Illustrate the intermolecular forces expected to be found in an oil-water+albumin interface
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(Please draw)
Illustrate the intermolecular forces expected to be found in an oil-water interface
Illustrate the intermolecular forces expected to be found in an oil-water+albumin
interface
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- Consider the intermolecular forces present in a pure sample of each of the following compounds: CH₃CH₂OH and CH₃COCH₃. Identify the intermolecular forces that these compounds have in common.(c) The figure below shows the measured osmotic pressure, II / c, against the mass concentration c of the polymer for polymer solutions A, B, C, and D. The temperature and solvent are constant. D П B A (i) Rank the polymers according to their molar mass. (ii) In which polymer solution is the quality of the solvent the poorest? What type of solvent is present in sample C? Explain your answer. (iii) Which polymers could have the same chemical composition Explain your answer.MW of LA Volume of NaOH used (ml) x Normality of NaOH x % t.a. (expressed as lactic acid)= 1000 x100 Volume or weight of sample (g or ml) Molecular Weight of Lactic Acid (MW of LA) = 90 g/mol %3D
- Mixtures of amino acids can be analyzed by first separating the mixture into its components through ion‑exchange chromatography. Amino acids placed on a cation‑exchange resin containing sulfonate (−SO−3)(−SO3−) groups flow down the column at different rates because of two factors that influence their movement: (1) ionic attraction between the sulfonate residues on the column and positively charged functional groups on the amino acids, and (2) aggregation of nonpolar amino acid side chains with the hydrophobic backbone of the polystyrene resin. Note that the ionic attraction is more important than hydrophobicity for this column media. For each pair of amino acids, identify which will be eluted first from a cation‑exchange column using a pH 7.0pH 7.0 buffer.Consider the following dipeptides: PC HE TG IR FL How many of the dipeptides in this group that would stick to an cation exchange column at pH %3D 8? Please give me the whole number as the answer, 0, 1, 2 etcWhat phosphate buffer conditions can be used to isolate protein (isoelectric point of 5.2) using anion exchanger? Using Henderson Hasselbach equation, show this buffer is made inluding calculations
- In a 0.1000 M acetic acid solution at 25 degrees celsius , the acid ionizes to the extent of about 1.34 %. Since each molecule of acetic acid which ionizes produces 1 H+ ion and 1 C2H3O2- ion, the concentration in the solution are: HC2H3O2 < -----------> H+ + C2H3O2-A mixture of proteins contains four different polypeptides, all in ~equal concentration, in solution with the following properties: Protein Molecular Mass (kDa) Isoelectric point A 45 4.5 B 77 6.0 C 28 4.1 D 14 10.7 A fraction of the protein solution is applied to a strong cation exchange column using a buffer at pH 8.0 with increasing [NaCl] from 0.05 M – 1.0 M. The chromatogram is shown below: 1. Based on the data presented, which of the following statements is true: Peak #1 is protein D Peak #4 is protein C Peak #3 is protein A Peak #4 is protein D Peak #2 is protein B 2. Since you know that the proteins are all present in approximately equal concentrations, the different relative peak areas tell you that: There are more neutral amino acids in protein #4…at 257 nm) is dissolved in 2.5 mL of buffer. A 250 microliter aliquot is removed and placed in a 1.0 cm A sample of adenosine triphosphate (ATP) (MW 507, ɛ = 14,700 M'cm cuvette with sufficient buffer to give a total volume of 2.0 mL. The absorbance of the sample at 257 nm is 2.0. Calculate the weight of ATP in the original 2.5 mL sample. (Choose the correct value from the drop-down list provided. The values of weight are listed in units of milligrams.) Weight of ATP: v mg
- The protein calcineurin binds to the protein calmodulin with an association rate of 8.9 × 103 M−1 s −1 and an overall dissociation constant, Kd, of 10 nM. Calculate the dissociation rate, kd , including appropriate units.Calculate the effective quantity (g) of sodium chloride related to tonicity in 100ml of an intravenous fluid labeled "5% dextrose in 0.45% sodium chloride," and indicate whether the solution is isotonic, hypotonic or hypertonic. The answer is Hypertonic and 1.35g NaCl but I don't understand how to get the answer.The simple form of |Hoff equation is: II = [B]RT In this equation the [B] is the molar concentration of solute. So: n m [B] = v MV = cg /MA Where c, the mass concentration of the solute is in the total volume of solution and M, is the molar mass of the solute. This equation can be replaced in the previous one to get: RT II = MA In this equation molar mass of given solute can be detemined from the slope of the II vs Cz plot. This equation applies only to solutions that are sufficiently dilute to behave as ideal-dilute solutions. In the case of non-ideal solutions, however, the extended formula is: II = [B]RT{1+ k. [B] + n. [B]² + ...} Biological macromolecules dissolve to produce solutions that are far from ideal, but we can still calculate the osmotic pressure by assuming that the van't Hoff equation is only the first term of a lengthier expression: II [B]RT(1+ b. [B]) II = RT + bRT. [B] [B] II = RT + bRT./M. */Ma п RT ÞRT Ca MA MA In this equation molar mass of given biomolecule can…