• DOI:10.1126/science.1853201
• Corpus ID: 11348405

A method to identify protein sequences that fold into a known three-dimensional structure.

@article{Bowie1991AMT,
  title={A method to identify protein sequences that fold into a known three-dimensional structure.},
  author={James U. Bowie and Roland L{\"u}thy and David S. Eisenberg},
  journal={Science},
  year={1991},
  volume={253 5016},
  pages={
          164-70
        }
}

• J. Bowie, R. Lüthy, D. Eisenberg
• Published 1991
• Biology
• Science

The inverse protein folding problem, the problem of finding which amino acid sequences fold into a known three-dimensional (3D) structure, can be effectively attacked by finding sequences that are most compatible with the environments of the residues in the 3D structure. The environments are described by: (i) the area of the residue buried in the protein and inaccessible to solvent; (ii) the fraction of side-chain area that is covered by polar atoms (O and N); and (iii) the local secondary structure. Examples of this 3D profile method are presented for four families of proteins: the globins, cyclic AMP (adenosine 3',5'-monophosphate) receptor-like proteins, the periplasmic binding proteins, and the actins. This method is able to detect the structural similarity of the actins and 70- kilodalton heat shock proteins, even though these protein families share no detectable sequence similarity.