Which of the following protein assays does not make use of the copper (I or II) ions in the determination of protein concentration? a. Biuret assay b. Bicinchoninic acid assay c. Bradford assay d. Lowry assay
Q: ОН S. NH2 HO NH2 Thyrosine (tyr) Methionine (met)
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A: T: Threonine, pKa: 9.0 S: Serine Y: Tyrosine, pKa: 10.0 M: Methionine C: Cysteine, pKa: 8.0 F:…
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A: Given peptide, CF C- Cysteine F - Phenylalanine
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A: The CO- NH bond is called peptide bond. A peptide bond connects two Amino acid units. Amino acid…
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Q: Calculate isoelectric point (PI) of the peptide GSTSRASPRM. pKa N-terminus = 9.3; pKa R = 12.5; pKa…
A: The peptide is GSTSRASPRM.
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Q: Choose true or false. Increase in temperature during ITC experiments can be used to determine the…
A: Introduction: ITC stands form Isothermal Titration Calorimetry. The technique is used to study the…
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Q: Examine the peptide. Thr‑Lys‑Pro‑Ile‑Val‑Ala‑Pro‑Met‑Glu‑Tyr‑Gly‑Lys Estimate the net charge on the…
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Q: Arginine has ionizable groups with pKa values of 2.17, 9.04, and 12.48. A researcher makes up 73 mL…
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Q: Calculate the pI of this peptide. Calculate the net charge of this peptide at pH 2, pH 7, and pH 11.
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Q: AMINO pKa1 pKa2 ACID Proline 1.99 10.96 Tryptophan 2.38 9.39 Valine 2.32 9.62 Glutamine 2.17 9.13…
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Q: The pKa values for Lysine are 1.92/ 9.99/13.8. At what pH will the amino acid not migrate in an…
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Q: Among these protein assays, which work in acidic conditions? a. Biuret assay b. Bicinchoninic acid…
A: Biuret assay works in alkaline medium, with the help of sodium potassium tartrate, it react with…
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- Use information from terminal residue analysis and partial hydrolysis to determine thestructure of an unknown peptide.Which separation technique is the most specific and offers the highest protein purification possible?Why is glycine the only amino acid commonly observed in peptides inconformations with phi and psi values which are not restricted to the values in the Ramachandran plot below?
- For standard turbidity measurements, the increase in signalis due toa.) higher amounts of analytes that complex with formazin.b.) higher amounts of analytes that precipitate with formazin.c.) higher amounts of analytes that react with formazin.For the determination of Pb in blood, a 5.00 mL sample was treated with trichloroacetic acid to precipitate the proteins. After centrifugation, the resulting solution was brought to pH 3 and extracted with two 5 mL portions of methyl isobutyl ketone containing the lead complexing agent APCD (ammonium 1-pyrrolidine carbodithiolate). The extract was drawn directly into an air-acetylene flame which produced an absorbance of 0.444 at 283.3 nm. Two 5.00 mL aliquots of solutions containing 0.250 and 0.450 ppm of Pb were subjected to the same sample treatment and the absorbance that occurred was 0.396 and 0.599 respectively. Calculate the concentration of Pb in µg/dL in the blood.Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and IIVD. None is true.pls explain
- I did not understand soultion for the question.. The relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 10³and 10⁵M, respectively. Which protein has the highest affinity for ligand ? Explain your reasoning. How do you make them all in same constant so that values can be compared and the one with highest Ka or lowest Kd (Highest affinity in both cases) can be ruled out.Consider the Blosum-62 matrix in Figure 6.9. Replacement of which three amino acids never yields a positive score? What features of these residues might contribute to this observation?. An Analytical Chemist is analyzing a protein sample analysis using a light scattering technique. If the formulation of the subject sample has included surfactants or salt additives, which of the following would adequately apply? . The additives would impact the ionic strength of the sample B. The impact of additives influence can be nullified when using a Light Scattering technique. C. The effect of formulation additives would impact the protein sample analysis, and should be considered as a factor when analyzing the protein aggregation using light scattering technique.
- An amino acid mixture of phenylalanine, glycine and glutamic acid is to be separated bypaper chromatography. The solvent is less polar than water. Which of these amino acids will have the highest Rf value and which the lowest? Explain. Treatment of a new protein with dansyl chloride reveals two (2) dansyl-labelled derivatives of amino acids, alanine and methionine. What can you deduce about the structure of the protein from these results? Name the amino acids that contribute atoms to both purine and pyrimidine rings.How many of the -amino acids shown in Table 26-1 contain aromatic rings? How many contain sulfur? How many contain alcohols? How many contain hydrocarbon side chains?If the pH of a solution of Arginine is equal to a half of the 3 pka values of all of its functional groups, what will be the charge on the majority of the Arg molecules in that solution? Please explain. Am i supposedd to add up the three pka values and then divide it in half to find the pH? Thanks