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

A method to identify protein sequences that fold into a known three-dimensional structure,Science,J. U. Bowie,R. Luethy,D. Eisenberg

A method to identify protein sequences that fold into a known three-dimensional structure   (Citations: 400)
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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: (1) the area of the residue buried in the protein and inaccessible to solvent; (2) the fraction of side-chain area that is covered by polar atoms (O and N); and (3) the local secondary structure. Examples of this 3D profile method are presented for four families of proteins: the globins, cyclic AMP (adenosine 3â²,5â²-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.
Journal: Science , vol. 253, no. 5016, pp. 164-170, 1991
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