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Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , |
| In: | Proceedings of the National Academy of Sciences, 70, 1973, 4, S. 1199-1203 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Walter, Roderich Glickson, J. D. Walter, Roderich Glickson, J. D. |
|---|---|
| author |
Walter, Roderich Glickson, J. D. |
| spellingShingle |
Walter, Roderich Glickson, J. D. Proceedings of the National Academy of Sciences Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin Multidisciplinary |
| author_sort |
walter, roderich |
| spelling |
Walter, Roderich Glickson, J. D. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.70.4.1199 <jats:p> The usefulness of 2,2,2-trifluoroethanol titration as a means of distinguishing between intramolecular peptide-peptide hydrogen bonding on the one hand and intermolecular peptide-peptide and peptide-solvent hydrogen bonding on the other has been investigated with neurohypophyseal hormones, and the results have been compared with those of other methods. The chemical shifts (220 MHz) of the resonances of amide N <jats:italic>H</jats:italic> and aromatic C <jats:italic>H</jats:italic> protons of oxytocin, lysine vasopressin, deamino-lysine vasopressin, and deamino-8-tosyllysine vasopressin were monitored as the solvent composition was progressively varied from 100% dimethylsulfoxide to 100% 2,2,2-trifluoroethanol. The overall backbone conformation of oxytocin appears to be retained, and possibly somewhat stabilized, during the solvent transition, while the backbone, particularly the acyclic component, of lysine vasopressin and its analogs is subject to solvent-induced perturbation. </jats:p> Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin Proceedings of the National Academy of Sciences |
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| title |
Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_unstemmed |
Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_full |
Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_fullStr |
Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_full_unstemmed |
Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_short |
Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_sort |
proton magnetic resonance study of peptide conformation: effect of trifluoroethanol on oxytocin and 8-lysine-vasopressin |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.70.4.1199 |
| publishDate |
1973 |
| physical |
1199-1203 |
| description |
<jats:p>
The usefulness of 2,2,2-trifluoroethanol titration as a means of distinguishing between intramolecular peptide-peptide hydrogen bonding on the one hand and intermolecular peptide-peptide and peptide-solvent hydrogen bonding on the other has been investigated with neurohypophyseal hormones, and the results have been compared with those of other methods. The chemical shifts (220 MHz) of the resonances of amide N
<jats:italic>H</jats:italic>
and aromatic C
<jats:italic>H</jats:italic>
protons of oxytocin, lysine vasopressin, deamino-lysine vasopressin, and deamino-8-tosyllysine vasopressin were monitored as the solvent composition was progressively varied from 100% dimethylsulfoxide to 100% 2,2,2-trifluoroethanol. The overall backbone conformation of oxytocin appears to be retained, and possibly somewhat stabilized, during the solvent transition, while the backbone, particularly the acyclic component, of lysine vasopressin and its analogs is subject to solvent-induced perturbation.
</jats:p> |
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| author | Walter, Roderich, Glickson, J. D. |
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| author_sort | walter, roderich |
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| description | <jats:p> The usefulness of 2,2,2-trifluoroethanol titration as a means of distinguishing between intramolecular peptide-peptide hydrogen bonding on the one hand and intermolecular peptide-peptide and peptide-solvent hydrogen bonding on the other has been investigated with neurohypophyseal hormones, and the results have been compared with those of other methods. The chemical shifts (220 MHz) of the resonances of amide N <jats:italic>H</jats:italic> and aromatic C <jats:italic>H</jats:italic> protons of oxytocin, lysine vasopressin, deamino-lysine vasopressin, and deamino-8-tosyllysine vasopressin were monitored as the solvent composition was progressively varied from 100% dimethylsulfoxide to 100% 2,2,2-trifluoroethanol. The overall backbone conformation of oxytocin appears to be retained, and possibly somewhat stabilized, during the solvent transition, while the backbone, particularly the acyclic component, of lysine vasopressin and its analogs is subject to solvent-induced perturbation. </jats:p> |
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| imprint | Proceedings of the National Academy of Sciences, 1973 |
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| spelling | Walter, Roderich Glickson, J. D. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.70.4.1199 <jats:p> The usefulness of 2,2,2-trifluoroethanol titration as a means of distinguishing between intramolecular peptide-peptide hydrogen bonding on the one hand and intermolecular peptide-peptide and peptide-solvent hydrogen bonding on the other has been investigated with neurohypophyseal hormones, and the results have been compared with those of other methods. The chemical shifts (220 MHz) of the resonances of amide N <jats:italic>H</jats:italic> and aromatic C <jats:italic>H</jats:italic> protons of oxytocin, lysine vasopressin, deamino-lysine vasopressin, and deamino-8-tosyllysine vasopressin were monitored as the solvent composition was progressively varied from 100% dimethylsulfoxide to 100% 2,2,2-trifluoroethanol. The overall backbone conformation of oxytocin appears to be retained, and possibly somewhat stabilized, during the solvent transition, while the backbone, particularly the acyclic component, of lysine vasopressin and its analogs is subject to solvent-induced perturbation. </jats:p> Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin Proceedings of the National Academy of Sciences |
| spellingShingle | Walter, Roderich, Glickson, J. D., Proceedings of the National Academy of Sciences, Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin, Multidisciplinary |
| title | Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_full | Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_fullStr | Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_full_unstemmed | Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_short | Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| title_sort | proton magnetic resonance study of peptide conformation: effect of trifluoroethanol on oxytocin and 8-lysine-vasopressin |
| title_unstemmed | Proton Magnetic Resonance Study of Peptide Conformation: Effect of Trifluoroethanol on Oxytocin and 8-Lysine-Vasopressin |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.70.4.1199 |