Backbone dynamics and structural characterization of the partially folded A state of ubiquitin by 1H, 13C, and 15N nuclear magnetic resonance spectroscopy.

@article{Brutscher1997BackboneDA,
  title={Backbone dynamics and structural characterization of the partially folded A state of ubiquitin by 1H, 13C, and 15N nuclear magnetic resonance spectroscopy.},
  author={Bernhard Brutscher and R. Br{\"u}schweiler and Richard R. Ernst},
  journal={Biochemistry},
  year={1997},
  volume={36 42},
  pages={13043-53}
}
Structure and dynamics of the partially folded A state of ubiquitin in a 60%/40% methanol/water mixture at pH 2 was studied by two- and three-dimensional nuclear magnetic resonance spectroscopy (NMR) using fully 13C,15N-labeled ubiquitin. Complete backbone 13CO, 13Calpha, 15N, and 1HN assignment was achieved. 13CO and 13Calpha chemical shifts and 1H-1H nuclear Overhauser enhancement (NOE) connectivities indicate different behavior for the N-terminal and the C-terminal halves of the protein. In… CONTINUE READING