A mixture of three peptides is provided to you. The sequences of the three peptides are known: 1. HHHHH (pl = 7.16) 2. wwwww (pl = 5.52) 3. YYYYE (pl= 4.00) Which of these three peptides would not have absorbance at 280 nm? Select all that apply Peptide 1 Peptide 2 Peptide 3 Which of the following purification protocols would best separate the three peptides in question #4 without using denaturing conditions? Size exclusion and hydrophobic interaction chromatography O Anion exchange chromatography and hydrophobic interaction chromatography O Maltose-affinity chromatography and isoelectric focusing O SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and anion exchange chromatography

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The globular proteins tend to have a high-dimensional folding in their higher-order structure g providing very limited analysis when conducting peptide analysis. Explain what steps would be suitable to prepare a successful chromatographic peptide mapping?

Can you please help find the ph 9.5 of ser?

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calculate the volume of stock solutions required to make up the buffer solutions that will be used for protein purification. The solutions you need to prepare for purification are: i. Binding Solution A: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 5mM imidazole, 5% (v/v) glycerol ii. Wash Solution B: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 75mM imidazole, 5% (v/v) glycerol iii. Elution Solution C: make up 10 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 500 mM imidazole, 5% (v/v) glycerol please show your working . Thnk you

You are given an equimolar (0.10 mM) mixture of Ubiquitin protein that is free/pure of any other macromolecules (e.g. nucleic acids) in a pH 7.0 phosphate buffer How can you purify Ubiquitin? Propose a 2-step minimum plan to purify their protein. Basic rules:  Affinity chromatography (e.g. His Tag purification) is not an allowed step because these proteins are in their native state (i.e. – do not have a polyhistidine tag). Also, you are not allowed to rely solely on the color of certain proteins (e.g. cytochrome C and GFP) in your characterization/proposal. You are allowed to buffer exchange (i.e. – switch buffers) but try to keep your pH’s in a reasonable range (5.5 – 8.5) or you risk denaturing your protein! Assume you can only separate proteins under 50.0 kDa with a 5.0 kDa difference using SEC. Otherwise, assume proteins greater than 50.0 kDa are unable to be separated. Assume proteins with the same charge (positive or negative) are not easily separated using IEC. Assume all…

Which of the peptide sequences below best matches the hydropathy plot shown? 1. ILYYAGSREDHSGYLIL 2. RAFLILFMTYFLILFLI 3. LHGDQNRERDGHSQERD 4. LIFLAIFPAGSTSEDRR 5. EQSDTERNQHGALIYLI

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