Integration of genome data and protein structures: prediction of protein folds, protein interactions and "molecular phenotypes" of single nucleotide polymorphisms

Curr Opin Struct Biol. 2001 Feb;11(1):125-30. doi: 10.1016/s0959-440x(00)00175-5.


With the massive amount of sequence and structural data being produced, new avenues emerge for exploiting the information therein for applications in several fields. Fold distributions can be mapped onto entire genomes to learn about the nature of the protein universe and many of the interactions between proteins can now be predicted solely on the basis of the genomic context of their genes. Furthermore, by utilising the new incoming data on single nucleotide polymorphisms by mapping them onto three-dimensional structures of proteins, problems concerning population, medical and evolutionary genetics can be addressed.

Publication types

  • Review

MeSH terms

  • Apolipoproteins E / chemistry
  • Apolipoproteins E / genetics
  • Forecasting / methods
  • Genomics / methods*
  • Models, Theoretical
  • Phenotype
  • Polymorphism, Single Nucleotide*
  • Protein Binding*
  • Protein Folding*
  • Sequence Homology, Amino Acid


  • Apolipoproteins E