Calculate the isoelectric point of tyrosine using the pKa values in Table 4-1 of Voet, Voet and Pratt.  6 options: 5.705 9.835 5.660 6.330

Enz-SH + Ag* - Enz-S-Ag + H* The affinity of Ag* for sulfhydryl groups is so great that Ag* can be used to titrate -SH groups quantitatively. To 10.0 mL of a solution containing 3.5 mg/mL of a pure enzyme, an investigator added just enough AGNO, to completely inactivate the enzyme. A total of 0.536 umol AGNO, was required. Calculate the minimum molecular weight (M,) of the enzyme. minimum M, = The determined M, is not exact, but it is a minimum value for the M, of the enzyme. Why does the M, value obtained this way give only the minimum molecular weight? There is only one polypeptide chain. There are no disulfide bonds in the protein. There is only one titratable -SH group per protein molecule. The Ag* would also react with the terminal carboxyl group.

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Peptides can be separated using an ion-exchange column based on their isoelectric (pl) values. At which pH values would two different peptides, one with a pl of 5.6 and the other with a pl of 9.1, bind to a cation- and anion-exchange column? Each peptide may be capable of binding to each column at more than one pH value. anion-exchange column at pH = 3.1 pH = 7.2 pH = 10.6 ****** cation-exchange column at pH = 3.1 pH = 7.2 PH =10.6 Answer Bank peptide B pl = 9.1 peptide A pl = 5.6

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The pKa values for Lysine are 1.92/ 9.99/13.8.   At what pH will the amino acid not migrate in an electrical field? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 10.9 b 9.8 c 11.9 d 9.7 e 8.4 f 11.2 g 10.6 h 11.6 i 11.1   im thinking answer is c please clarify

At what pH will the amino group of threonine be 50% deprotonated? The pKa values of threonine are 2.2, 9.8 and 13 O 13 O 56 O 22

Draw a resonance structure, complete with all formal charges and lone (unshared) electron pairs, that shows the resonance interaction of the amino with the ortho position in aniline. NH₂ aniline • You do not have to consider stereochemistry. • Include all valence lone pairs in your answer. • In cases where there is more than one answer, just draw one. My 3 $390.05 Jn [F +▼

0.9 The enzyme from the previous problem was further purified from the supernatant, after which a (Bradford) protein assay using coomassie blue was performed. The following standard curve was established using known concentrations of the enzyme. 595 0.8 0.7 0.6 0.5 80.4 0.3 0.2 0.1 y=0.5617x+0.0119 R²=0.9878 0 0.5 Protein Concentration (mg/mL) A. At what wavelength is the sample measured at? 1.5 B. Write out the equation relating OD595 and protein concentration. C. After purification, the protein sample was diluted 10-fold and then reacted with Coomassie Blue that resulted in an OD595 of 0.7. What was the concentration of protein in the supernatant? D. The purified protein was concentrated to a final volume of 1 L. What was the final amount of purified protein recovered? 200 g of the hulls initially at 25°C was placed into a perfectly insulated calorimeter with 500 g of isopropyl alcohol (IPA) at 5°C without stirring. At equilibrium, the temperature of the IPA was found to be 13.7°C. =…

Which of the following amino acids is most likely to have a positively-charged side group under normal physiological pH conditions? O a. Lysine O b. Alanine O c. Leucine O d. Glycine O e. Aspartic acid Next page Previous page Time left 1:33:55 Quiz navigation 271 PM 今 D 572 2022 DELL Delete PgUp PgDn F12 PrtScr Insert F9 F10 F11 F7 F8 F5 F6 F2 F3 F4 Esc F1 Backspace & % %3D @ # 8 6 7 3 1 Y Enter J K A s D F ck St