Draw a fractional binding curve (θ v.s [L]) for a protein binding to one molecule of L with a Kd of 10 mM.
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Draw a fractional binding curve (θ v.s [L]) for a protein binding to one molecule of L with a Kd of 10 mM.
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- Given the following Peptide: Q6 *H;N-Phe-Asp-Ala-Arg-Gy-His-Arg-Asp-Glu-His-Tyr-CO 6a. What is the peptide's net charge at pH 2.0, pH 6.0, pH 7.4, and pH 10.2? (show work) 6b. What is the approximate isoelectric point of this peptide?Determine the net charge (to the nearest integer) on the following peptide at pH 5 AND pH 12. Estimate the isoelectric point (pl) for this peptide: H2N-Leu-Gly-Lys-Glu-COOH Assume the pK,s for functional groups are: alpha-amino 6. alpha-carboxy sidechain-amino (Lys) 10.5 sidechain-carboxy (Glu) 4.2 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =6.6 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =3.1 O Net charge at plH 5 and 12 is +2 and -1, respectively, pl =7.5 O Nct charge at pH 5 and 12 is +1 and -1. respectively,. pl -4.5 2.Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.
- 12 mM of protein A is combined with 6 mM of ligand X in water. After the protein-ligand complex binding reaches equilibrium, you measure that the free ligand concentration is 3 mM and the concentration of protein-ligand complex is 3 mM. What is the Kd for protein A? Although they would be in mM, do not include units in your answer, only the number as a whole integer.Protein concentration can readily be determined using the Beer-Lambert law: A = e l c where A = absorbance e = molar absorption coefficient (M-1cm-1) l = light path length (cm) c = concentration (M) If the molar absorption coefficient at 280 nm for yeast ADH is 48860 M-1cm-1 and a 10 mL solution of the protein has an absorbance at 280 nm of 0.4 (as measured by a spectrometer with pathlength 1 cm), then what is the concentration of the protein solution (in μM)? i.e. concentration = ______ μM If the molecular weight of the protein is 36849, what is its concentration in mg/mL? i.e. concentration = _______ mg/mL For each part of the question, show your calculations to arrive at your answers.You have purified Protein 'X' and you want to know its concentration. As we learned, you can calculate concentrations by simply measuring UV280 absorbance of protein solutions. Using a UV spectrophotometer, you measured an absorbance of 0.6. Given that Protein X has an absorptivity (or extinction coefficient) of 0.2 mL•mg-cm at 280 nm, what is the concentration of purified protein solution (assume the light path is 1 cm)? -1 O A. 3 g/mL B. 3 mg/mL OC.0.2mg/mL OD.0.2 g/mL OE. 0.6 g/mL
- An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.Calculate θ for a certain protein-ligand pair when the ligand concentration = 1 M and the Kd = 1 X 10-15 M.Draw Glu-His-Trp-Ser-Gly-Leu-Arg-Pro-Gly peptide. What is the net charge of this peptide at pH 3, 8 and 11? What can you say about pI value of this peptide?
- The process of a protein folding from an inactive unfolded structure to theactive folded structure can be represented by the following equation: unfolded protein ⇌ folded proteinThe values of ΔH° and ΔS° for the folding of the protein lysozyme are: ΔH ° = -280 kJ/ mol ΔS ° = -790 J/mol • K(a) Calculate the value of ΔG° for the folding of lysozyme at 25 °C.(b) At what temperature would you expect the unfolding of lysozyme tobecome favorable? (c) At what temperature would the ratio of unfolded protein to foldedprotein be 1:5?The amino acid arginine ionizes according to the following scheme: NH₂ I C=N I ΝΗ Part A pl = Submit H (CH₂)3 H-N-C-COOH II HH 1 [ΠΙ ΑΣΦ H H Calculate the isoelectric point of arginine. Express your answer using three significant figures. Request Answer pk-2.17 -H* +H* wwwww NH₂ C=N ΝΗ H (CH₂)3 1 ? H H-N-C-COO- | | H H 11 H pk-8.99 -H* +H* NH₂ I C=N I ΝΗ T (CH₂)3 H H H₂N-C-COO- I H pk - 12.5 -H* +H* NH₂ C=N=H NH I (CH₂)3 H₂N-C-COO- I H IVGive the general Adiar equation for the binding of a ligand to a dimeric protein. Explain further what your understanding is of the terms "no-, positive-, and negative cooperativity” and graphically present the relationship between Ȳ and [S] for each of these cases. Also, give the relationship between the constants Kb1 and Kb2 in each case.