Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry.

@article{Chetty2012ApolipoproteinAH,
  title={Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry.},
  author={Palaniappan Sevugan Chetty and Leland Mayne and Zhong-yuan Kan and Sissel Lund-Katz and S. Walter Englander and Michael C Phillips},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2012},
  volume={109 29},
  pages={11687-92}
}
To understand high-density lipoprotein (HDL) structure at the molecular level, the location and stability of α-helical segments in human apolipoprotein (apo) A-I in large (9.6 nm) and small (7.8 nm) discoidal HDL particles were determined by hydrogen-deuterium exchange (HX) and mass spectrometry methods. The measured HX kinetics of some 100 apoA-I peptides specify, at close to amino acid resolution, the structural condition of segments throughout the protein sequence and changes in structure… CONTINUE READING
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