Electrospray can transfer the peptide from solution into the gas-phase while retaining the peptides charge state from solution. Based on the MGDH peptide's acidic and basic sites what will be the main overall charge state of the peptide at pH 1, 3, 5, 7 and 11?
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- A peptide was analyzed with the following results. What is the primary structure of the peptide? State what each experimental result reveals about the structure and indicate your logic. a) Amino acid analysis: R, C (2 equivalents), G, I, H, M, Y, Vb) After one round of Edman degradation, a mixture of glycine and isoleucine were detected. c) Treatment with beta-mercaptoethanol yielded two peptides, a 4-mer and a 5-mer.Which method of chromatography would be the most appropriate for separating mixtures of thefollowing peptides at a neutral pH? (a) ARDDEKLLML, LMYWWILLDETSARALIV, DQNNA(b) GATSKKIVLM, ASCILLVMEN, MFDDAAYVNE(c) KLMDAATSPFLMAGHHHHHH, MFPSATEKRQQNNESTVLAG In what order would the following peptides be eluted from an anion exchange column at pH 7.5?Peptide 1: Ala–Asp–Glu–Gln–Trp–Leu–His–ValPeptide 3: Phe–Gln–Glu–Ala–Gln–His–Leu–Arg-IlePeptide 2: Arg–Ile–Pro–Lys–Cys–Met–LysBefore high performance liquid chromatography (HPLC) methods were devised for the separation and analysis of small peptides, electrophoresis on a paper support was frequently used. Separation was affected on the basis of the charge on a peptide at different pH values. a. What is the charge of the primary structure of proteins at pH = 2.0, 4.0, 6.0 and 11.0 of the following proteins. Draw their structures and predict their net charge. i.) Lys- Gly- Ala- Glyii.) Lys- Gly-Ala-Gluiii.) His- Gly- Ala- Gluiv.) Glu- Gly- Ala -Gluv.) Gln-Gly-Ala-Lys b.) Calculate the pI of the following primary structure of protein c.) the migration toward the cathode, the negative pole; A for the migration toward the anode,the positive pole; and O if the peptide remains stationary.
- A postgraduate student was given the task of predicting the 1H NMR spectrum for compound A. Compound A is one of the basic amino acid. Tripeptide B is formed through a condensation process between compounds A, C, and D, while monomers E and F are formed by modifying compounds C and A by maintaining the basic structure of amino acid. Compounds C and D are neutral and acidic amino acids, respectively. The addition reaction of monomers E and F forms polymer G. (a) Illutsrate the potential 1H NMR spectrum for compound A. (b) Identify the possible structural formula of compound A (according to the type of hydrogen and carbon) based on your proposed 1H NMR spectrum. (c) Identify the possible structural formula of compounds B, C, D, E, F and G. (d) Identify the possible structural formula for repeating unit of polymer G. (e) Discuss the differences between compound C and cyclic alcohol."Regarding resolution of mass spectrometers and various ways mass of peptides can be represented, which is or are true? " "A larger peptides will have a smaller difference between the monoisotopic and average masses, compared to smaller peptides, because the contribution of 13C is greater. " Higher resolution allows investigators to distinguish between monoisotopic masses and other masses of otherwise identical peptides. "Average mass size is always smaller than monoisotopic mass, because 13C and 15N contribute to monoisotopic mass. " "Monoisotopic mass is calculated as if there are no heavy isotopes within the peptide, and so is always smaller than the average observed mass."There is parts A-D for the picture provided. A) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 1? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 B) A peptide has the sequence Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 5? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 C) Same Peptide sequence, What is the net charge at pH8.5, (N-terminus is pronated) Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 D) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 13? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 Thank You!
- The amino acid sequence of three peptide fragments are shown below. Peptide 1: QAMGRAGDLKYLGLHSV Peptide 2: ALMALFMVMALVLVSVLFIA Peptide 3: MVEDLLKQIARYLISE (a) Circle all of the charged residues in peptide 1 (assume pH =7.0). Box all of the aromatic residues in peptide 2. Underline all of the nonpolar residues in peptide 3. (b) Determine the net charge of the predominant form of each of the peptides at pH 4.5 and pH 11.5. Assume the ionizable groups have the pKa values listen in Table 2.1 of your text. (c) Which of these peptides would be most likely to be found as an alpha helix in a soluble (cytoplasmic) protein? Which would be most likely to be found as an alpha helix in a transmembrane protein? Which would be least likely to form an alpha helix of any kind?At pH 7.0, in what order would the following three peptides (described by their amino acid composition) be eluted from a column filled with a cationexchange polymer?Peptide A: Ala 10%, Glu 5%, Ser 5%, Leu 10%, Arg 10%, His 5%, Ile 10%, Phe 5%, Tyr 5%, Lys 10%, Gly 10%, Pro 5%, and Trp 10%.Peptide B: Ala 5%, Val 5%, Gly 10%, Asp 5%, Leu 5%, Arg 5%, Ile 5%, Phe 5%, Tyr 5%, Lys 5%, Trp 5%, Ser 5%, Thr 5%, Glu 5%, Asn 5%, Pro 10%, Met 5%, and Cys 5%.Peptide C: Ala 10%, Glu 10%, Gly 5%, Leu 5%, Asp 10%, Arg 5%, Met 5%, Cys 5%, Tyr 5%, Phe 5%, His 5%, Val 5%, Pro 5%, Thr 5%, Ser 5%, Asn 5%, and Gln 5%Deduce the amino acid sequence of a polypeptide from the following:1. Acid hydrolysis gives Ala2, Arg, Lys2, Met, Phe, Ser22. Carboxypeptidase gives Ala3. Trypsin digestion gives 4 peptides a) Ala, Arg b) Lys, Phe, Ser c) Lys d) Ala, Met, Ser4. CNBr treatment gives a) Ala, Arg, Lys2, homoserine, Phe, Ser b) Ala, Ser5. Thermolysin is a protease that cuts on the N-terminal side of hydrophobic amino acids (substrate preference is Leu, Ile, Phe, Trp, Tyr, Val). Thermolysin treatment of our polypeptide yields 2 peptides a) Ala, Arg, Ser b) Ala, Lys2, Met, Phe, Ser
- the peptide sequence in single letter code is T N C H P, please hand draw a peptide diagram satisfied the following conditions * Show the position of all ‘heavy’ atoms with the appropriate letter (C, N, O, S etc.) and indicate the number of attached hydrogen atoms (no skeletal structures allowed). * Show all double bonds and/or partial double bonds. * Draw all ionisable groups as their most highly populated state at pH 7. * Make the peptide bond between the fourth residue and proline the cis isomer. * Show all other peptide bonds as trans. * Show the alpha carbon of every residue as tetrahedral and the L isomer. * All trigonal planar groups must be shown explicitly with appropriate geometry. 2. Give the name and three letter code for each amino acid in the peptide. 3. At pH 7, approximately what charge would be on your peptide? Explain your answer. 4. Can your peptide form intra/interchain disulfide bonds? Explain why/why not. 5. Will your peptide absorb UV (either strongly, weakly…Given below are sequences of amino acids present in an oligo-peptide chain. Count the overall charge of each assigned peptide and write it in your answer. Along with it also mention that toward which electrode (cathode or anode) will the peptide move? Please remember that cathode is a negativeelectrode and anode is a positive electrode. Ile-Lys-Arg-Trp-Lys-Asn-Glu-His-Pro-Asp-Ala-Tyr-Phe-Glu-Met-Phe-Gly-ValA researcher has synthesized two peptides and needs to confirm whether the peptides were synthesized with the correct sequence using mass spectrometry. What is the sequence of the b4 and y7 ions for peptide GAMECHANGER? The peptide SLISRAEFLAGVRVGV is digested with trypsin. Then the products of the digestion are subjected to ESI TOF-MS in positive ion mode with the peptides in a pH 2 solution. What peptide fragments will result and what are their m/z?