How Good Are Simplified Models for Protein Structure Prediction?. (29th April 2014)

• Record Type: Journal Article
• Authors: Shatabda, Swakkhar; Newton, M. A. Hakim; Rashid, Mahmood A.; Pham, Duc Nghia; Sattar, Abdul
• Other Names: Dasgupta Bhaskar Academic Editor.
• Is Part Of: Advances in bioinformatics. Volume 2014(2014)
• Publication Date: 2014-04-29
• Subjects: Bioinformatics -- Periodicals; Bioinformatics; Computational Biology -- Periodicals; Periodicals; 570.285
• DOI: 10.1155/2014/867179
• Languages: English
• ISSNs: 1687-8027

Abstract

Abstract : Protein structure prediction (PSP) has been one of the most challenging problems in computational biology for several decades. The challenge is largely due to the complexity of the all-atomic details and the unknown nature of the energy function. Researchers have therefore used simplified energy models that consider interaction potentials only between the amino acid monomers in contact on discrete lattices. The restricted nature of the lattices and the energy models poses a twofold concern regarding the assessment of the models. Can a native or a very close structure be obtained when structures are mapped to lattices? Can the contact based energy models on discrete lattices guide the search towards the native structures? In this paper, we use the protein chain lattice fitting (PCLF) problem to address the first concern; we developed a constraint-based local search algorithm for the PCLF problem for cubic and face-centered cubic lattices and found very close lattice fits for the native structures. For the second concern, we use a number of techniques to sample the conformation space and find correlations between energy functions and root mean square deviation (RMSD) distance of the lattice-based structures with the native structures. Our analysis reveals weakness of several contact based energy models used that are popular in PSP.