Probing the lipid-free structure and stability of apolipoprotein A-I by mutation.

@article{Gorshkova2000ProbingTL,
  title={Probing the lipid-free structure and stability of apolipoprotein A-I by mutation.},
  author={Irina N Gorshkova and Kyriaki Liadaki and Olga Gursky and David Atkinson and Vassilis I. Zannis},
  journal={Biochemistry},
  year={2000},
  volume={39 51},
  pages={
          15910-9
        }
}
To probe the secondary structure of the C-terminus (residues 165-243) of lipid-free human apolipoprotein A-I (apoA-I) and its role in protein stability, recombinant wild-type and seven site-specific mutants have been produced in C127 cells, purified, and studied by circular dichroism and fluorescence spectroscopy. A double substitution (G185P, G186P) increases the protein stability without altering the secondary structure, suggesting that G185 and G186 are located in a loop/disordered region. A… CONTINUE READING

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