C-N CH Proline 2 CH2 0 CH2 CH2 CH2 CH2 listidine aspertetc SH Cy steine H2 NH2 L

Question

C-N CH Proline 2 CH2 0 CH2 CH2 CH2 CH2 listidine aspertetc SH Cy steine H2 NH2 LuSine 2. Could the peptide above be detected by UV absorbance in a spectrophotometer? Why? Doesn+ contain tryptophanNo 3. Consider the following peptide to answer the questions below. Gly-Asp-Glu-Ala Glycine pKa's: 2,9 Aspartate pKa's: 1.9,9.6,3.7 Glutamate pKa's: 2.2,9.7, 4.3 Alanine pKa's: 2.3,9.7 A) At pH 7, could the peptide bind to an ion echange chromatography column? B) Should the resin within the column be negatively or positively charged? C) How could you could elute the peptide from the column? t. A mixture of 3 proteins, under native conditions, are added to a size exclusion column: Hemoglobin, molecular mass 64,000 Daltons (1 Dalton 1 g/mol) FosB, molecular mass 45,000 Daltons WNK1, molecular mass 230,000 Daltons Recall that hemoglobin has four subunits. Each subunit is ~16000 Daltons. FosB and WNK1 have only one subunit. In what order will the proteins elute from the column?

Explanation / Answer

2)no it will not be observed in the UV because it donot contains the aromatic amino acids which actually gives the uv absorbance..

3)(a) yes it can bind as it contains lysine and Histidine which will have the slightly positive charge over it due to the presence of aspartate a..

(b) the amino acids contain positive charge so the resins should have negative charge on them so that they can bind the positive amino acids .

(c) to elute that protein we have wash the attached resin in buffer having high pH so that the amino acids positive charge get neutral hence it will leave the resin..

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