Corpus ID: 20239379

Location of helical regions in tetrapyrrole-containing proteins by a helical hydrophobic moment analysis. Application to phytochrome.

@article{Parker1990LocationOH,
  title={Location of helical regions in tetrapyrrole-containing proteins by a helical hydrophobic moment analysis. Application to phytochrome.},
  author={W. Parker and P. S. Song},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 29},
  pages={
          17568-75
        }
}
  • W. Parker, P. S. Song
  • Published 1990
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • Helical regions in many tetrapyrrole proteins are highly amphiphilic, one side interacting with a hydrophobic core and another side interacting with the polar solvent. The mean helical hydrophobic moment is a measure of amphiphilicity of a helix. Helical regions in myoglobin, the alpha and beta subunits of C-phycocyanin, and cytochrome c can be distinguished from nonhelical regions by use of a hydrophobic moment analysis. 24 of 27 (89%) of the helical regions in these proteins were located by… CONTINUE READING
    21 Citations

    Topics from this paper.

    Structural domains of phytochrome deduced from homologies in amino acid sequences
    • 19
    Amphiphilic α-Helical Potential: A Putative Folding Motif Adding Few Constraints to Protein Evolution
    • 6
    • Highly Influenced
    Short-lived alpha-helical intermediates in the folding of beta-sheet proteins.
    • 11
    Localization of protein-protein interactions between subunits of phytochrome.
    • 71
    • PDF