Thermal unfolding of Apo and Holo Desulfovibrio desulfuricans flavodoxin: cofactor stabilizes folded and intermediate states.

@article{Muralidhara2004ThermalUO,
  title={Thermal unfolding of Apo and Holo Desulfovibrio desulfuricans flavodoxin: cofactor stabilizes folded and intermediate states.},
  author={Bilikallahalli K Muralidhara and Pernilla Wittung-Stafshede},
  journal={Biochemistry},
  year={2004},
  volume={43 40},
  pages={12855-64}
}
We here compare thermal unfolding of the apo and holo forms of Desulfovibrio desulfuricans flavodoxin, which noncovalently binds a flavin mononucleotide (FMN) cofactor. In the case of the apo form, fluorescence and far-UV circular dichroism (CD) detected transitions are reversible but do not overlap (T(m) of 50 and 60 degrees C, respectively, pH 7). The thermal transitions for the holo form follow the same pattern but occur at higher temperatures (T(m) of 60 and 67 degrees C for fluorescence… CONTINUE READING

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We here compare thermal unfolding of the apo and holo forms of Desulfovibrio desulfuricans flavodoxin , which noncovalently binds a flavin mononucleotide ( FMN ) cofactor .
We conclude that ( 1 ) a three - state thermal unfolding behavior appears to be conserved among long- and short - chain , as well as apo and holo forms of , flavodoxins and ( 2 ) flavodoxin 's thermal stability ( in both native and intermediate states ) is augmented by the presence of the FMN cofactor .
We here compare thermal unfolding of the apo and holo forms of Desulfovibrio desulfuricans flavodoxin , which noncovalently binds a flavin mononucleotide ( FMN ) cofactor .
We conclude that ( 1 ) a three - state thermal unfolding behavior appears to be conserved among long- and short - chain , as well as apo and holo forms of , flavodoxins and ( 2 ) flavodoxin 's thermal stability ( in both native and intermediate states ) is augmented by the presence of the FMN cofactor .
We here compare thermal unfolding of the apo and holo forms of Desulfovibrio desulfuricans flavodoxin , which noncovalently binds a flavin mononucleotide ( FMN ) cofactor .
We here compare thermal unfolding of the apo and holo forms of Desulfovibrio desulfuricans flavodoxin , which noncovalently binds a flavin mononucleotide ( FMN ) cofactor .
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