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Real-time observation of conformational fluctuations in Zn-substituted myoglobin by time-resolved transient hole-burning spectroscopy.
Equilibrium fluctuations of the protein conformation have been studied in myoglobin by a novel method of time-resolved transient hole-burning spectroscopy over a temperature range of 180-300 K and a time range of 10 ns to 10 ms. The temporal shift of the hole spectrum has been observed in a wide tem...
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| Autors principals: | , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
1998
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1299726/ https://ncbi.nlm.nih.gov/pubmed/9649414 |
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