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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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Bibliographische Detailangaben
Hauptverfasser: Damberger, F., Nikonova, L., Horst, R., Peng, G., Leal, W. S., Wüthrich, K.
Format: Artigo
Sprache:Inglês
Veröffentlicht: Cold Spring Harbor Laboratory Press 2000
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Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144629/
https://ncbi.nlm.nih.gov/pubmed/10850815
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