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.
%0 Journal Article
%1 citeulike:432190
%A Bowie, J. U.
%A Lüthy, R.
%A Eisenberg, D.
%C Molecular Biology Institute, University of California, Los Angeles 90024-1570.
%D 1991
%J Science
%K design, post-defense, prediction, profiles, structure
%N 5016
%P 164--170
%T A method to identify protein sequences that fold into a known three-dimensional structure.
%U http://view.ncbi.nlm.nih.gov/pubmed/1853201
%V 253
%X 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.
@article{citeulike:432190,
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.},
added-at = {2009-05-19T18:00:18.000+0200},
address = {Molecular Biology Institute, University of California, Los Angeles 90024-1570.},
author = {Bowie, J. U. and L\"{u}thy, R. and Eisenberg, D.},
biburl = {https://www.bibsonomy.org/bibtex/2693ff631c3345b13caa89820290320bf/earthfare},
citeulike-article-id = {432190},
description = {CiteULike: Everyone's library},
interhash = {418e8148e7394104be8296e57dc9227a},
intrahash = {693ff631c3345b13caa89820290320bf},
issn = {0036-8075},
journal = {Science},
keywords = {design, post-defense, prediction, profiles, structure},
month = {July},
number = 5016,
pages = {164--170},
posted-at = {2009-05-19 03:27:20},
priority = {2},
timestamp = {2009-05-19T18:03:27.000+0200},
title = {A method to identify protein sequences that fold into a known three-dimensional structure.},
url = {http://view.ncbi.nlm.nih.gov/pubmed/1853201},
volume = 253,
year = 1991
}