An algorithm to generate low-resolution protein tertiary structures from knowledge of secondary structure.
- 24 May 1994
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 91 (11) , 5027-5029
- https://doi.org/10.1073/pnas.91.11.5027
Abstract
An algorithm is described to assemble the three-dimensional fold of a protein starting from its secondary structure. A reduced representation of the polypeptide chain is used together with a crude potential based on pair hydrophobicities. The method is shown to be successful in locating the native topology for two 4-alpha-helix bundles, myohemerythrin and cytochrome b-562.Keywords
This publication has 18 references indexed in Scilit:
- Reduced representation model of protein structure prediction: Statistical potential and genetic algorithmsProtein Science, 1993
- Structure-derived hydrophobic potentialJournal of Molecular Biology, 1992
- Prediction of protein backbone conformation based on seven structure assignmentsJournal of Molecular Biology, 1991
- Protein folding bottlenecks: A lattice Monte Carlo simulationPhysical Review Letters, 1991
- Simulations of the Folding of a Globular ProteinScience, 1990
- Structure of myohemerythrin in the azidomet state at resolutionJournal of Molecular Biology, 1987
- Improvement of the 2.5 Å resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphicsJournal of Molecular Biology, 1981
- On the prediction of protein structure: The significance of the root-mean-square deviationJournal of Molecular Biology, 1980
- Protein folding: Evaluation of some simple rules for the assembly of helices into tertiary structures with myoglobin as an exampleJournal of Molecular Biology, 1979
- Protein-folding dynamicsNature, 1976