Structure and Function of Subunit a of the ATP Synthase of Escherichia coli

@article{Vik2005StructureAF,
  title={Structure and Function of Subunit a of the ATP Synthase of Escherichia coli},
  author={Steven B. Vik and Robert R. Ishmukhametov},
  journal={Journal of Bioenergetics and Biomembranes},
  year={2005},
  volume={37},
  pages={445-449}
}
 The structure of subunit a of the Escherichia coli ATP synthase has been probed by construction of more than one hundred monocysteine substitutions. Surface labeling with 3-N-maleimidyl-propionyl biocytin (MPB) has defined five transmembrane helices, the orientation of the protein in the membrane, and information about the relative exposure of the loops connecting these helices. Cross-linking studies using TFPAM-3 (N-(4-azido-2,3,5,6-tetrafluorobenzyl)-3-maleimido-propionamide) and… CONTINUE READING
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