Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis.

ABSTRACT: 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 were introduced by an amber codon and a four-base codon respectively. Eight double-labeled proteins were prepared, purified, and subjected to FRET analysis in 6 M urea. The observed behavior could be explained by a power law, R = αN0.44, where R, and N are the distance and the number of residues betw

SUBMITTER: Yamaguchi M 

PROVIDER: S-EPMC5899696 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature