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NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori.
NMR spectroscopic changes as a function of pH in solutions of the pheromone-binding protein of Bombyx mori (BmPBP) show that BmPBP undergoes a conformational transition between pH 4.9 and 6.0. At pH below 4.9 there is a single "acid form" (A), and a homogeneous "basic form" (B) e...
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| Auteurs principaux: | , , , , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
Cold Spring Harbor Laboratory Press
2000
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2144629/ https://ncbi.nlm.nih.gov/pubmed/10850815 |
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