Structural characterization and pH-induced conformational transition of full-length KcsA.

@article{Zimmer2006StructuralCA,
  title={Structural characterization and pH-induced conformational transition of full-length KcsA.},
  author={Jochen Zimmer and Declan A Doyle and J. G{\"u}nter Grossmann},
  journal={Biophysical journal},
  year={2006},
  volume={90 5},
  pages={1752-66}
}
The bacterial K+ channel KcsA from Streptomyces lividans was analyzed by neutron and x-ray small-angle solution scattering. The C-terminally truncated version of KcsA, amenable to crystallographic studies, was compared with the full-length channel. Analyzing the scattering data in terms of radius of gyration reveals differences between both KcsA species of up to 13.2 A. Equally, the real-space distance distribution identifies a 40 to 50 A extension of full-length KcsA compared to its C… CONTINUE READING

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