Denaturation studies by fluorescence and quenching of thermophilic protein NAD+-glutamate dehydrogenase from Thermus thermophilus HB8.

@article{Ruiz2003DenaturationSB,
  title={Denaturation studies by fluorescence and quenching of thermophilic protein NAD+-glutamate dehydrogenase from Thermus thermophilus HB8.},
  author={Jos{\'e} L. Ruiz and Juan F Sanguesa Ferrer and Carmen Pire and Francisco I Llorca and Mar{\'i}a-Jos{\'e} Bonete},
  journal={Journal of protein chemistry},
  year={2003},
  volume={22 3},
  pages={295-301}
}
Fluorescence techniques have been used to study the structural characteristics of many proteins. The thermophilic enzyme NAD-glutamate dehydrogenase from Thermus thermophilus HB8 is found to be a hexameric enzyme. Fluorescence spectra of native and denatured protein and effect of denaturants as urea and guanidine hydrochloride on enzyme activity of thermophilic glutamate dehydrogenase (t-GDH) have been analyzed. Native t-GDH presents the maximum emission at 338 nm. The denaturation process is… CONTINUE READING