Coupling the folding of homologous proteins.
The empirical observation that homologous proteins fold to similar structures is used to enhance the capabilities of an ab initio algorithm to predict protein conformations. A penalty function that forces homologous proteins to look alike is added to the potential and is employed in the coupled energy optimization of several homologous proteins. Significant improvement in the quality of the computed structures (as compared with the computational folding of a single protein) is demonstrated and discussed.
Keasar
C
C
Department of Physical Chemistry, Department of Biological Chemistry, Fritz Haber Research Center for Molecular Dynamics and Wolfson Center for Applied Structural Biology, Hebrew University, Givat Ram Jerusalem 91904, Israel.
Tobi
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D
Elber
R
R
Skolnick
J
J
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008962:Models, Theoretical; D008969:Molecular Sequence Data; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D011506:Proteins