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Hiding in plain sight: three chemically distinct α -helix types.

Shuguang ZhangMartin Egli
Published in: Quarterly reviews of biophysics (2022)
Linus Pauling in 1950 published a three-dimensional model for a universal protein secondary structure motif which he initially called the alpha-spiral. Jack Dunitz, then a postdoc in Pauling's lab suggested to Pauling that the term helix is more accurate than spiral when describing the right-handed peptide and protein coiled structures. Pauling agreed, hence the rise of the alpha-helix, and, by extension, the ‘double helix’ structure of DNA. Although structural biologists and protein chemists are familiar with varying polar and apolar characters of amino acids in alpha-helices, to non-experts the three chemically distinct alpha-helix types classified here may hide in plain sight.
Keyphrases
  • amino acid
  • dna binding
  • protein protein
  • high resolution
  • binding protein
  • preterm infants
  • systematic review
  • randomized controlled trial
  • transcription factor
  • cell free
  • circulating tumor
  • gestational age
  • preterm birth