Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer.

@article{Farrow1995ComparisonOT,
  title={Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer.},
  author={Neil Alexander Farrow and O S Zhang and Julie Deborah Forman-Kay and Lewis E. Kay},
  journal={Biochemistry},
  year={1995},
  volume={34 3},
  pages={
          868-78
        }
}
Two-dimensional NMR 15N relaxation studies have been used to characterize the backbone dynamics and folding transition of the N-terminal SH3 domain of the protein drk (drkN SH3). The isolated drkN SH3 domain exists in equilibrium between a folded and an unfolded state in aqueous buffer and near neutral pH [Zhang et al. (1994) J. Biomol. NMR 4, 845]. The backbone dynamics of both the folded and unfolded states in this exchanging system have been determined and the rates of the folding transition… CONTINUE READING
BETA

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 50 CITATIONS

Similar Papers

Loading similar papers…