Concanavalin (ConA) is a 25.5KDa protein with pl of 4.7 and optical absorbance (A 0.1% 289) of 1.14. calculate the concentration of an aqueous solution of pure BSA protein with an absorbance of 0.66 at 280nm. give your answer in units of mg/ml ?
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- 80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.Calculate the concentration of 0.2ml amino acid when path length is 1cm and has an absorbance value of 0.50, if a 0.5ml solution of same amino acid has a concentration of 0.72mg/ml with an absorbance of 0.9.80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCL needed to reach relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
- Calculate the unknown concentration of the PROTEIN C with an absorbance value of A412 given the standard curve indicated in the table below. Write your final answer (NUMBER ONLY) in two decimal places rounded off. Protein concentration (µg/mL) 0 0.02 0.04 0.06 0.08 0.10 Your answer APIENT Absorbance 0.000 0.161 0.284 0.438 0.572 0.762If your initial absorbance from undiluted crude dialysate is 4.50, determine the fold dilution needed to yield an absorbance of approximately 0.700. If you want to prepare 1.0 ml of diluted crude, what volume (mL) of crude dialysate must you add? Your Answer: Answer units It is possible to estimate the molar extinction coefficient of a protein from knowledge of its amino acid composition, as shown from your experiences with EXPASY. From the molar extinction coefficient of tyrosine, tryptophan and cystine (cysteine does not absorb appreciably at wavelengths >260 nm, while cystine does) at a given wavelength, the extinction coefficient of the native protein in water can be computed using the following equation: e(Protein) = #(Tyr)*E(Tyr) + #(Trp)*E(Trp) + #(Cystine)*E(Cystine) Where (if A280 measured in water): E (Tyr) = 1490, ɛ (Trp) = 5500, e (Cystine) = 125 Estimate the molar extinction coefficient of lysozyme using the above equation and the amino acid composition data you found…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
- Protein Solubility 3.5 5.5 5 5 0.068 0.028 Absorbance 0.098 Conc.(mg/ml) 0.195 0.130 0.044 0.9% 2.786% 9.429% 11.3: % solubility 4.179% The above table indicates the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH. Dilution Factor 30 22.5 15 PH 7.5 1.5 4.5 5 0.027 3 0.042 Protein Solubility Versus pH 6.5 6 4.5 pH Value The above figure shows a plot of protein solubility versus pH. 50 7.5 7.5 50 0.032 0.053 8.5 50 0.054 0.100 21.429% 9 Please provide a brief discussion and explanation of the results. (using isoelectric point and net charge to explain)Assuming the molar extinction coefficient for para-nitrophenyl phosphate (PNP) is 55,290 mol "dm cm, calculate the concentration of the molecule that produced an absorbance of 0.770 OD units in a 1.5 cm cuvette. Show all working -1 3 -1The-carotene molecule has λmax 450 nm and ɛ = 15.000 m2 / mol. Calculate the expected absorbance value for a solution in which 0.1 mg is dissolved in 10 mL of water. ( β-carotene, C40H56, 536 g/mol path length 1 cm)
- A protein gives, under conditions of buffer composition, pH, and temperaturethat are close to physiological conditions, a molecular weight by size exclusion measurements of 140,000 g/mol. When the same protein is studiedby SDS gel electrophoresis in the absence or presence of the reducing agent β-mercaptoethanol (BME), the patterns seen, respectively, in lanes A and B are observed. Lane C contains standards of molecular weight indicated. From these data, describe the native protein, in terms of the kinds of subunits present, the stoichiometry of subunits, and the kinds of bonding(covalent, noncovalent) existing between subunits.Consider the titration of 30.0 mL of 0.0700 M HONH2 (a weak base; Kb = 1.10e-08) with 0.100 M HI. Calculate the pH after the following volumes of titrant have been added: (a) 0.0 mLpH = (b) 5.3 mLpH = (c) 10.5 mLpH = (d) 15.8 mLpH = (e) 21.0 mLpH = (f) 27.3 mLpH =A protein gives, under conditions of buffer composition, pH, and temperature that are close to physiological conditions, a molecular weight by sedimentation equilibrium measurements of 140,000 g/mol. When the same protein is studied by SDS gel electrophoresis in the absence or presence of the reducing agent β-mercaptoethanol (BME), the patterns seen in lanes A and B respectively are observed. Lane C contains standards of molecular weight indicated. From these data, describe the native protein, in terms of the kinds of subunits present, the stoichiometry of subunits (that is, how many of each subunits are present), and the kinds of bonding (covalent, non-covalent) existing between subunits