A method to identify protein sequences that fold into a known three-dimensional structure
- Univ. of California, Los Angeles (United States)
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 3{prime},5{prime}-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.
- OSTI ID:
- 5826882
- Journal Information:
- Science (Washington, D.C.); (United States), Journal Name: Science (Washington, D.C.); (United States) Vol. 253:5016; ISSN SCIEA; ISSN 0036-8075
- Country of Publication:
- United States
- Language:
- English
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