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Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect
Data are reported for T(m), the temperature midpoint of the thermal unfolding curve, of ribonuclease A, versus pH (range 2–9) and salt concentration (range 0–1 M) for two salts, Na(2)SO(4) and NaCl. The results show stabilization by sulfate via anion-specific binding in the concentration range 0–0.1...
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| Hauptverfasser: | , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
Cold Spring Harbor Laboratory Press
2002
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2373655/ https://ncbi.nlm.nih.gov/pubmed/12070329 |
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