Abstract
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.
Keywords
Structural similarityProtein secondary structureProtein structureGlobinProtein foldingPeptide sequenceBiochemistryLoop modelingChemistryBiologyProtein structure predictionComputational biologyBiophysicsHemoglobin
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Publication Info
- Year
- 1991
- Type
- article
- Volume
- 253
- Issue
- 5016
- Pages
- 164-170
- Citations
- 2783
- Access
- Closed
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Cite This
James U. Bowie,
Roland Lüthy,
David Eisenberg
(1991).
A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure.
Science
, 253
(5016)
, 164-170.
https://doi.org/10.1126/science.1853201
Identifiers
- DOI
- 10.1126/science.1853201