Involvement of Electrostatic Interactions in the Mechanism of Peptide Folding Induced by Sodium Dodecyl Sulfate Binding†,‡
✍ Scribed by Montserret, Roland; McLeish, Michael J.; Böckmann, Anja; Geourjon, Christophe; Penin, François
- Book ID
- 115314817
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 351 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0006-2960
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## Abstract Circular dichroism spectra have been obtained for tri(L‐lysine), tetra(L‐lysine), and penta(L‐lysine) in aqueous sodium dodecyl sulfate at 25°C. None of the oligomers are affected significantly by sodium dodecyl sulfate at detergent concentrations exceeding 0.01 __M__. Literature result
The premise that one manifestation of the nexus between Sertoli cells and germ cells may be an orderly and sequential change in their protein profiles has been examined in relation to the ontogeny of spermatogenesis in the colony-bred albino rat. Viable "Sertoli cell-germ cell associations"1 isolate