Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol.

@article{Buck1995CharacterizationOC,
  title={Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol.},
  author={Matthias Buck and Harald Schwalbe and Christopher M. Dobson},
  journal={Biochemistry},
  year={1995},
  volume={34 40},
  pages={13219-32}
}
2D and 3D heteronuclear NMR methods have been used to characterize the structure of hen egg-white lysozyme in a partially folded state using uniformly 15N-labeled protein. This state is formed by the denaturation of the protein in 70% trifluoroethanol (TFE)/30% water (v/v) and is characterized by substantial helical secondary structure in the absence of extensive tertiary interactions. 15N-filtered 3D NOESY and TOCSY experiments have allowed the sequential assignment of resonances for all but 2… CONTINUE READING

From This Paper

Topics from this paper.
16 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 16 extracted citations

Similar Papers

Loading similar papers…