Rotational motion of rhodamine 6G tethered to actin through oligo(ethylene glycol) linkers studied by frequency-domain fluorescence anisotropy

Investigation of the rotational motion of a fluorescent probe tethered to a protein helps to elucidate the local properties of the solvent and protein near the conjugation site of the probe. In this study, we have developed an instrument for frequency-domain fluorescence (FDF) anisotropy measurement...

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Detalles Bibliográficos
Autores principales: Wazawa, Tetsuichi, Morimoto, Nobuyuki, Nagai, Takeharu, Suzuki, Makoto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society of Japan (BSJ) 2015
Materias:
Regular Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736842/
https://www.ncbi.nlm.nih.gov/pubmed/27493858
http://dx.doi.org/10.2142/biophysico.12.0_87

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736842/
https://www.ncbi.nlm.nih.gov/pubmed/27493858
http://dx.doi.org/10.2142/biophysico.12.0_87

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