Uncoupling hydrophobicity and helicity in transmembrane segments. Alpha-helical propensities of the amino acids in non-polar environments.

@article{Li1998UncouplingHA,
  title={Uncoupling hydrophobicity and helicity in transmembrane segments. Alpha-helical propensities of the amino acids in non-polar environments.},
  author={L{\`i}jiāng Li{\'u} and Charles M. Deber},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 37},
  pages={23645-8}
}
Although the chains of amino acids in proteins that span the membrane are demonstrably helical and hydrophobic, little attention has been paid toward addressing the range of helical propensities of individual amino acids in the non-polar environment of membranes. Because it is inappropriate to apply soluble protein-based structure prediction algorithms to membrane proteins, we have used de novo designed peptides (KKAAAXAAAAAXAAWAAXAAAKKKK-amide, where X indicates one of the 20 commonly… CONTINUE READING

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Uncoupling Hydrophobicity and Helicity

  • D. T. Jones, W. R. Taylor, J. M. Thornton
  • Biochemistry
  • 1994
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