Predicting coiled coils from protein sequences

Science. 1991 May 24;252(5009):1162-4. doi: 10.1126/science.252.5009.1162.


The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry
  • Animals
  • Databases, Factual
  • Humans
  • Probability
  • Protein Conformation*
  • Proteins / chemistry
  • Proteins / genetics*


  • Amino Acids
  • Proteins