Time-resolved emission spectroscopy to elucidate the functional nature of heat-stable transcription factor

A 22 kDa protein from Thermus thermophilus is characterised as a DNA binding transcription regulator and its function is established using the fluorescence spectroscopy technique. The steady-state fluorescence spectroscopy result shows significant binding of calf thymus DNA and protein molecule. To confirm, the DNA quenching effect in real-time, a time-resolved emission spectroscopy study was performed and the result shows good agreement with steady-state quenching analysis. © 2022 Wiley Periodicals LLC.

Авторы
Kutumbarao N.V. 2, 1 , Karthikeyan S. 4, 5, 3 , Ganesan S. 3 , Velmurugan D. 1, 6
Journal
Journal of Cellular Biochemistry
Язык
English
Статус
Published
Ссылка
Внешняя ссылка
DOI
10.1002/JCB.30266
Год
2022
Организации
  • 1 Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Tamil Nadu, Chennai, India
  • 2 Institute of Transformative Bio-Molecules (ITbM), Nagoya University, Nagoya, Japan
  • 3 Department of Medical Physics, Anna University, Tamil Nadu, Chennai, India
  • 4 Department of Organic Chemistry, Science Faculty, Peoples’ Friendship University of Russia (RUDN University), Moscow, Russian Federation
  • 5 School of Advanced Sciences, Physics Division, Vellore Institute of Technology University, Chennai Campus, Tamil Nadu, Chennai, India
  • 6 Department of Biotechnology, School of Bioengineering, SRM Institute of Science and Technology, Tamil Nadu, Kattankulathur, India
Ключевые слова
calf thymus (ct) DNA; purification; Thermus thermophilus; time correlated single photon counting
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