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Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics
Mechanisms that regulate the nitric oxide synthase enzymes (NOS) are of interest in biology and medicine. Although NOS catalysis relies on domain motions, and is activated by calmodulin binding, the relationships are unclear. We used single-molecule fluorescence resonance energy transfer (FRET) spec...
Αποθηκεύτηκε σε:
| Τόπος έκδοσης: | Proc Natl Acad Sci U S A |
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| Κύριοι συγγραφείς: | , , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
National Academy of Sciences
2015
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4586839/ https://ncbi.nlm.nih.gov/pubmed/26311846 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1508829112 |
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