Functional consequences of alterations to hydrophobic amino acids located in the M4 transmembrane sector of the Ca(2+)-ATPase of sarcoplasmic reticulum.

@article{Clarke1993FunctionalCO,
  title={Functional consequences of alterations to hydrophobic amino acids located in the M4 transmembrane sector of the Ca(2+)-ATPase of sarcoplasmic reticulum.},
  author={David R. Clarke and T. Y. Wings Loo and William E. Pine Kenneth H. Pollock Joseph E. Hightower Tho Rice and Jens P Andersen and Bente Vilsen and David MacLennan},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 24},
  pages={18359-64}
}
Those hydrophobic residues between Ile298 and Ile315 in transmembrane segment M4 of the Ca(2+)-ATPase of sarcoplasmic reticulum, not previously mutated, were mutated systematically in ways that would alter their size or polarity, and functional consequences were measured. Fourteen residues in this sequence are organized as juxtapositions of large, hydrophobic (Val, Leu, Ile) and small (Ala, Gly) residues, and these were altered so that large residues were substituted for small and vice versa… CONTINUE READING