algorithm to generate low-resolution protein tertiary structures from knowledge of secondary structure

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 t...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1994-05, Vol.91 (11), p.5027-5029
Main Authors: Monge, A, Friesner, R.A, Honig, B
Format: Article
Language:English
Subjects:
Algorithms
Atoms
Biochemistry
Biophysics
Cytochrome b Group - chemistry
Cytochromes
Escherichia coli Proteins
Force field
Gyration
Hemerythrin - analogs & derivatives
Hemerythrin - chemistry
Local minimum
molecular conformation
polypeptides
prediction
Protein folding
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Simulated annealing
structure
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Description
Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.91.11.5027