## Abstract ^1^H NMR spectra of the dipiperazine‐based DNA minor groove binding compound Hoechst 32985 indicate that at room temperature and low pH (2.90) a single conformation is detected. This is attributed to the form in which both piperazine rings are protonated at the __N__‐methyl and the bulk
Effects of pH and temperature on cardioactive polypeptides from sea anemones: A 1H-nmr study
✍ Scribed by Paul R. Gooley; John W. Blunt; Laszlo Beress; Raymond S. Norton
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1988
- Tongue
- English
- Weight
- 866 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The effects of pH and temperature on the 300-MHz 'H-nmr spectra of three cardioactive polypeptides from sea anemones, anthopleurin-A from Anthopleura zunthogrammicu (AP-A) and Ammonia sukutu toxins I and I1 (ATX I and 11), are described. AP-A and ATX I1 exhibit major spectral heterogeneity. Evidence from the pH and temperature studies and from high performance liquid chromatography indicates that this heterogeneity is conformational rather than chemical in origin. By contrast, purified isotoxins of ATX I show no evidence of conformational heterogeneity. The pKa values of most of the ionizable groups in these polypeptides are not strongly perturbed by interactions in the tertiary structure, with the exception of one of the Asp carboxylates, which has a pKa of 5 2 in AP-A and ATX I1 and 3.0 in ATX I. Protonation of this carboxylate, suggested to be Asp-9, leads to a conformational change in all three molecules. All three polypeptides are thermally stable, showing some conformational changes but not major unfolding at elevated temperatures.
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