Protein secondary structure and homology by neural networks. The alpha-helices in rhodopsin

FEBS Lett. 1988 Dec 5;241(1-2):223-8. doi: 10.1016/0014-5793(88)81066-4.

Abstract

Neural networks provide a basis for semiempirical studies of pattern matching between the primary and secondary structures of proteins. Networks of the perceptron class have been trained to classify the amino-acid residues into two categories for each of three types of secondary feature: alpha-helix or not, beta-sheet or not, and random coil or not. The explicit prediction for the helices in rhodopsin is compared with both electron microscopy results and those of the Chou-Fasman method. A new measure of homology between proteins is provided by the network approach, which thereby leads to quantification of the differences between the primary structures of proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Models, Neurological*
  • Models, Theoretical*
  • Molecular Sequence Data
  • Protein Conformation*
  • Retinal Pigments*
  • Rhodopsin*

Substances

  • Retinal Pigments
  • Rhodopsin