Structural organization of the N-terminal domain of apolipoprotein A-I: studies of tryptophan mutants.

@article{Davidson1999StructuralOO,
  title={Structural organization of the N-terminal domain of apolipoprotein A-I: studies of tryptophan mutants.},
  author={W. Sean Davidson and K Arnvig-McGuire and April L Kennedy and Jeffrey Kosman and Theodore L. Hazlett and Ana Jonas},
  journal={Biochemistry},
  year={1999},
  volume={38 43},
  pages={14387-95}
}
Site-directed mutagenesis and detailed fluorescence studies were used to study the structure and dynamics of recombinant human proapolipoprotein (proapo) A-I in the lipid free state and in reconstituted high-density lipoprotein (rHDL) particles. Five different mutants of proapoA-I, each containing a single tryptophan residue, were produced in bacteria corresponding to each of the naturally occurring Trp residues (position -3 in the pro-segment, 8, 50, 72, and 108) in the N-terminal half of the… CONTINUE READING

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