Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis.
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ABSTRACT:
SUBMITTER: Yamaguchi M
PROVIDER: S-EPMC5899696 | biostudies-literature | 2018 Apr
REPOSITORIES: biostudies-literature
Publications
Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis.
Yamaguchi Mariko M Ohta Emi E Muto Takuya T Watanabe Takayoshi T Hohsaka Takahiro T Yamazaki Yoichi Y Kamikubo Hironari H Kataoka Mikio M
Biophysical reviews 20171125 2
Structural characterization of fully unfolded proteins is essential for understanding not only protein-folding mechanisms, but also the structures of intrinsically disordered proteins. Because an unfolded protein can assume all possible conformations, statistical descriptions of its structure are most appropriate. For this purpose, we applied Förster resonance energy transfer (FRET) analysis to fully unfolded staphylococcal nuclease. Artificial amino acids labeled with a FRET donor or acceptor w ...[more]
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