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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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Detalhes bibliográficos
Main Authors: Ramos, Carlos H.I., Baldwin, Robert L.
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 2002
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2373655/
https://ncbi.nlm.nih.gov/pubmed/12070329
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