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 ener...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1998-05, Vol.95 (11), p.5880-5883
Main Authors: Keasar, Chen, Tobi, Dror, Elber, Ron, Skolnick, Jeff
Format: Article
Language:English
Subjects:
Algorithms
Amino Acid Sequence
Animals
Biochemistry
Coordinate systems
Energy
Humans
Models, Molecular
Models, Theoretical
Molecular Sequence Data
Papers from Colloquium
Penalty function
Protein Folding
Proteins
Proteins - chemistry
Sequence Homology, Amino Acid
Simulated annealing
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.95.11.5880