(ii) 2. You are given two ESI-MS m/z spectra (in positive ionisation mode) of a protein recorded under different conditi

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answerhappygod
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(ii) 2. You are given two ESI-MS m/z spectra (in positive ionisation mode) of a protein recorded under different conditi

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Ii 2 You Are Given Two Esi Ms M Z Spectra In Positive Ionisation Mode Of A Protein Recorded Under Different Conditi 1
Ii 2 You Are Given Two Esi Ms M Z Spectra In Positive Ionisation Mode Of A Protein Recorded Under Different Conditi 1 (74.26 KiB) Viewed 35 times
Ii 2 You Are Given Two Esi Ms M Z Spectra In Positive Ionisation Mode Of A Protein Recorded Under Different Conditi 2
Ii 2 You Are Given Two Esi Ms M Z Spectra In Positive Ionisation Mode Of A Protein Recorded Under Different Conditi 2 (39.03 KiB) Viewed 35 times
(ii) 2. You are given two ESI-MS m/z spectra (in positive ionisation mode) of a protein recorded under different conditions (pH 7 and pH 2). All the peaks you observe in the spectra are due to the protein carrying different numbers of charges. () Look at the two spectra and describe the differences you observe between them as directed in the worksheet. With relation to protein structure What typically happens to a protein when you put it into a solution at low pH? (iii) Suggest why you observe a greater number of m/z peaks in the spectrum recorded of the protein at pH 2. (iv) Determine the molecular weight of the protein at pH 7 using peak A9. (peak A9 has 9 charges on it) Determine the molecular weight of the protein at pH 2 using peak A9. (peak A9 has 9 charges on it) (vi) Deduce what metal ion was bonded to the protein in its native state.
Question 2; ESI spectrum of a protein at pH7 and pH2 AR14549 100 AR1616 pH 7 A11455 1490715130 AL13213 1676 17 18 VE 100 A10031 17A A 149555 A1: PH 2 A 10104 AT11162 411 116 A1013392 A: 1487.9 000 10g 1000 110 1200 1300 100 1500 1000 7700 1800
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