(a)
To determine: The structure of the phenylthiohydantoin derivative of alanine.
Interpretation: The structure of the phenylthiohydantoin derivative of alanine is to be determined.
Concept introduction: The process in which a proper series of amino acids is maintained in the peptide chain is known as edmann degradation. this process includes the labelling of terminal amino residue followed by the cleavage of this terminal amino residue from the peptide chain. the peptide bonds between other amino acids do not get disturb during this process.
(b)
To determine: The structure of the phenylthiohydantoin derivative of tryptophan.
Interpretation: The structure of the phenylthiohydantoin derivative of tryptophan is to be determined.
Concept introduction: The process in which a proper series of amino acids is maintained in the peptide chain is known as edmann degradation. this process includes the labelling of terminal amino residue followed by the cleavage of this terminal amino residue from the peptide chain. the peptide bonds between other amino acids do not get disturb during this process.
(c)
To determine: The structure of the phenylthiohydantoin derivative of lysine.
Interpretation: The structure of the phenylthiohydantoin derivative of lysine is to be determined.
Concept introduction: The process in which a proper series of amino acids is maintained in the peptide chain is known as edmann degradation. this process includes the labelling of terminal amino residue followed by the cleavage of this terminal amino residue from the peptide chain. the peptide bonds between other amino acids do not get disturb during this process.
(d)
To determine: The structure of the phenylthiohydantoin derivative of proline.
Interpretation: The structure of the phenylthiohydantoin derivative of proline is to be determined.
Concept introduction: The process in which a proper series of amino acids is maintained in the peptide chain is known as edmann degradation. this process includes the labelling of terminal amino residue followed by the cleavage of this terminal amino residue from the peptide chain. the peptide bonds between other amino acids do not get disturb during this process.
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Organic Chemistry, Books a la Carte Edition (9th Edition)
- 5. Use the MS data to answer the questions on the next page. 14.0 1.4 15.0 8.1 100- MS-IW-5644 26.0 2.8 27.0 6.7 28.0 1.8 29.0 80 4.4 38.0 1.0 39.0 1.5 41.0 1.2 42.0 11.2 43.0 100.0 44.0 4.3 79.0 1.9 80.0 2.6 Relative Intensity 40 81.0 1.9 82.0 2.5 93.0 8.7 20- 95.0 8.2 121.0 2.0 123.0 2.0 136.0 11.8 0 138.0 11.5 20 40 8. 60 a. Br - 0 80 100 120 140 160 180 200 220 m/z Identify the m/z of the base peak and molecular ion. 2 b. Draw structures for each of the following fragments (include electrons and charges): 43.0, 93.0, 95.0, 136.0, and 138.0 m/z. C. Draw a reasonable a-fragmentation mechanism for the fragmentation of the molecular ion to fragment 43.0 m/z. Be sure to include all electrons and formal charges. 6. Using the values provided in Appendix E of your lab manual, calculate the monoisotopic mass for the pyridinium ion (CsH6N) and show your work.arrow_forwardNonearrow_forwardStereochemistry: Three possible answers- diastereomers, enantiomers OH CH₂OH I -c=0 21108 1101 41745 HOR CH₂OH IL Но CH₂OH TIL a. Compounds I and III have this relationship with each other: enantiomers b. Compounds II and IV have this relationship with each other: c. Compounds I and II have this relationship with each other: d. *Draw one structure that is a stereoisomer of II, but neither a diastereomer nor an enantiomer. (more than one correct answer)arrow_forward
- Don't used Ai solutionarrow_forwardDon't used Ai solutionarrow_forwardIn mass spectrometry, alpha cleavages are common in molecules with heteroatoms. Draw the two daughter ions that would be observed in the mass spectrum resulting from an alpha cleavage of this molecule. + NH2 Q Draw Fragment with m/z of 72arrow_forward
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