Hydrodynamic properties of Vibrio harveyi acyl carrier protein and its fatty-acylated derivatives.

@article{Roche1997HydrodynamicPO,
  title={Hydrodynamic properties of Vibrio harveyi acyl carrier protein and its fatty-acylated derivatives.},
  author={M A de la Roche and Zhitao Shen and David M. Byers},
  journal={Archives of biochemistry and biophysics},
  year={1997},
  volume={344 1},
  pages={159-64}
}
The amino acid sequence of Vibrio harveyi acyl carrier protein (ACP) is 86% identical to that of Escherichia coli ACP, although five nonconservative amino acid differences are concentrated in the loop region between helices I and II (residues 18-25). We have investigated the influence of these sequence differences on the hydrodynamic properties of the two ACPs and their fatty acylated derivatives. Hydropathy analysis suggests that V. harveyi ACP is more hydrophobic than E. coli ACP in the loop… CONTINUE READING

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