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Ligand binding and thermodynamic stability of a multidomain protein, calmodulin.
Chemical and thermal denaturation of calmodulin has been monitored spectroscopically to determine the stability for the intact protein and its two isolated domains as a function of binding of Ca2+ or Mg2+. The reversible urea unfolding of either isolated apo-domain follows a two-state mechanism with...
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| Autores principales: | , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
Cold Spring Harbor Laboratory Press
2000
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2144730/ https://ncbi.nlm.nih.gov/pubmed/10975573 |
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