On the nature of interaction of dodecyl sulfate with proteins. Evidence from uncharged polypeptides
| Autor: | Ezzat S. Younathan, Donald K. Igou, Jung-Teh Lo, Donald S. Clark, Wayne L. Mattice |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Circular dichroism
Dodecyl sulfate Protein Conformation Glutamine Biophysics macromolecular substances Biochemistry Drug Stability stomatognathic system Polymer chemistry Organic chemistry Equilibrium dialysis Molecular Biology Binding Sites Aqueous solution Chemistry Circular Dichroism Temperature technology industry and agriculture Proteins Sodium Dodecyl Sulfate Water Cell Biology Hydrogen-Ion Concentration Kinetics Solubility Spectrophotometry Ultraviolet Peptides Dialysis Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 60:140-145 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(74)90183-1 |
| Popis: | Circular dichroism and equilibrium dialysis measurements in aqueous solution reveal no strong interaction between dodecyl sulfate and the unionized polypeptides poly(N5-ω-hydroxyethyl-L-glutamine), poly(N5-ω-hydroxypropyl-L-glutamine) and poly(N5-bis(ω-hydroxyethyl)-L-glutamine). Dodecyl sulfate does not affect the stability of the helical forms of poly(N5-ω-hydroxypropyl-L-glutamine) and poly(N5-bis(ω-hydroxyethyl)-L-glutamine) in water. |
| Databáze: | OpenAIRE |
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