Abstract

An approach based exclusively on finding the global minimum of an appropriate potential energy function has been used to predict the unknown structures of five globular proteins with sizes ranging from 89 to 140 amino acid residues. Comparison of the computed lowest-energy structures of two of them (HDEA and MarA) with the crystal structures, released by the Protein Data Bank after the predictions were made, shows that large fragments (61 residues) of both proteins were predicted with rms deviations of 4.2 and 6.0 Å for the C α atoms, for HDEA and MarA, respectively. This represents 80% and 53% of the observed structures of HDEA and MarA, respectively. Similar rms deviations were obtained for ∼60-residue fragments of the other three proteins. These results constitute an important step toward the prediction of protein structure based solely on global optimization of a potential energy function for a given amino acid sequence.

Keywords

Amino acid residueGlobular proteinProtein structureProtein structure predictionPeptide sequenceFunction (biology)Amino acidCrystallographyProtein Data BankBiological systemChemistryPhysicsBiologyBiochemistryGenetics

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Year
1999
Type
article
Volume
96
Issue
10
Pages
5482-5485
Citations
206
Access
Closed

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Adam Liwo, Jooyoung Lee, Daniel R. Ripoll et al. (1999). Protein structure prediction by global optimization of a potential energy function. Proceedings of the National Academy of Sciences , 96 (10) , 5482-5485. https://doi.org/10.1073/pnas.96.10.5482

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DOI
10.1073/pnas.96.10.5482