Ab initio 3-D structure predictionof an artificially designed three-α-helix bundlevia all-atom molecular dynamics simulations

A. Breda, D.S. Santos, L.A. Basso2,3, O. Norberto de Souza
Published October 05, 2007
Genet. Mol. Res. 6 (4): 901-910 (2007)

About the authors
A. Breda, D.S. Santos, L.A. Basso2,3, O. Norberto de Souza

Corresponding author
O. Norberto de Souza
E-mail: osmar.norberto@pucrs.br


The rate at which knowledge about genomic sequences and their protein products is produced is increasing much faster than the rate of 3-dimensional protein structure determination by experimental methods, such as X-ray diffraction and nuclear magnetic resonance. One of the major challenges in structural bioinformatics is the conversion of genomic sequences into useful information, such as characterization of protein structure and function. Using molecular dynamics (MD) simulations, we predicted the 3-dimensional structure of an artificially designed three-α-helix bundle, called A3, from a fully extended initial conforma tion, based on its amino acid sequence. The MD protocol enabled us to obtain the secondary, in 1.0 ns, as well as the supersecondary and tertiary structures, in 4.0-10.0 ns, of A3, much faster than previously described for a similar protein system. The structure obtained at the end of the 10.0-ns MD simulation was topologically a three-α-helix bundle.

Key words: Ab initio prediction, Three-α-helix bundle, Molecular dynamics simulations, Protein 3-D structure 

Back To Top