Indicate the net charge of cysteine at pH 9.5
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Indicate the net charge of cysteine at pH 9.5
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- The free energy of hydrolysis for acetic anhydride is221.8 kJ/ mol. The conversion of ATP to ADP also involvesthe cleavage of an anhydride bond. Its free energy of hydrolysis is 230 kJ/ mol. Explain the difference in these values.The net charge on the most prevalent form of bisphosphoglycerate in blood is what?The α-amylase (α-AM) enzyme secreted by Aspergillus has an isoelectric point of approximately 4.2. If the purification method in problem 1 operates at pH 6.5, would the protein carry a positive charge, negative charge, or net zero charge?
- At pH 7, tryptophan crosses a lipid bilayer at about onethousandththe rate of indole, a closely related compound: Suggest an explanation for this observation.Paper electrophoresis of Asn, Ala, Asp, Lys and Ser mixtures at pH = 7 shows the fastest movement towards the anode The fully saponified 10g oil sample consumed 1.87g KOH, and the iodine value of the oil was 28.3. So how many unsaturated double bonds are there in each oil molecule on average? (lodine is known to have an atomic weight of 127) Given that 100g cellulose sample is completely hydrolyzed to obtain 78g glucose, then the percentage of cellulose in the sample is _% Given that the Km of catalase is 20mmol/L and the substrate concentration is 80mmol/L, then the percentage of catalase bound to the substrate is %Sketch the appearance after visualization of a protein mixture containing the seven proteins (fibrinogen, y-globulin, collagen, ovalbumin, myoglobin, hemoglobin, insulin) when subjected to two-dimensional (2D) gel electrophoresis.
- A series of standard proteins and an unknown enzyme were studied by gel filtration on a Sephadex G200 (the 200 refers to the maximum pore size in kDa) column. The elution volume Vel for each protein is given in Table 1 below. (a) Plot the data in the form of log Mr versus elution volume. From the line of best fit through the points for the standards, determine the Mr of the unknown enzyme. Explain why ferritin and ovomucoid behave anomalously. Table 1 - The Vel versus Mr data Protein Mr Vel (mL) Blue dextran* Lysozyme Chymotrypsin Ovalbumin Serum albumin Aldolase Urease Ferritin# Ovomucoid# Unknown 1,000,000 14,000 25,000 45,000 68,500 150,000 500,000 700,000 28,000 ⎯ 85 200 190 170 150 125 90 92 160 139 *Blue dextran is not a protein but a high-Mr carbohydrate that has a covalently bound blue dye, and it elutes with the void volume of the column. # Do not…Organic polymers have a similar composition to that of common carbohydrates(predominantly composed of Carbon, Hydrogen and Oxygen atoms). By principle, somecarbohydrates readily react with oxygen gas to produce carbon dioxide and water vapor,explain why this principle doesn’t spontaneously work on organic polymer wastes such asPolyethylene terepththalate (PET) and Polystyrene (PS)?The isoelectric point, pI, of the protein deoxyribonuclease I is 10.2 , while that of pepsin is 1. What is the net charge of deoxyribonuclease I at pH 7.3 ? What is the net charge of pepsin at pH 3.5 ? The isoelectric point of tryptophan is 5.89 ; phenylalanine , 5.48 . During paper electrophoresis at pH 6.5 , toward which clectrode does tryptophan migrate? During paper electrophoresis at pH 4.5, toward which electrode does phenylalanine migrate? [
- The pKa for histidine is pKa = 6.1 while that for cysteine is pKa = 8.0 2. Assume that both histidine and cysteine are catalytic groups for a particular enzyme. Assume also that the side chain of cysteine must be in the deprotonated form. Estimate the pH at which the catalytic activity of this enzyme is the maximum and sketch a pH-activity graph.Amino acids, such as glycine, are the key building blocks of proteins and will be discussed in greater detail in Chapter 25. At the pH of the stomach, glycine exists predominantly in a protonated form in which there are two acidic protons of interest. The pKa values for these protons are shown. Using this information, draw the form of glycine that will predominate at physiological pH of 7.4.An enzyme uses a lysine and a histidine as general acid-base catalytic residues. In one direction of the reaction, the lysine and histidine residues are typically protonated (~NH3*, ~Im), but in the other direction of the reaction, the two residues are "reverse protonated" (~NH2, ~Hlm*) (see below scheme). A pH profile of the reaction at various pH values yielded estimates of 7.57 and 9.30 for the macroscopic ionization constants pk,' and pK2, respectively. A separate set of experiments with site-speciffic variants of the enzyme yielded an estimate of 8.78 for the microscopic ionization constant pKp. Given this information, what is the value of the microscopic ionization constant pKA? Report your answer to the nearest hundredth. Lys-NH3* His-HIm" KB H KA H* Lys-NH2 Lys-NH3* His-HIm" His-Im Kc H* Kp Lys-NH2 His-Im