This paper presents a two-level protein folding optimization on a three-dimensional AB off-lattice model. The first level is responsible for forming conformations with a good hydrophobic core or a set of compact hydrophobic amino acid positions. These conformations are forwarded to the second level, where an accurate search is performed with the aim of locating conformations with the best energy value. The optimization process switches between these two levels until the stopping condition is satisfied. An auxiliary fitness function was designed for the first level, while the original fitness function is used in the second level. The auxiliary fitness function includes expression about the quality of the hydrophobic core. This expression is crucial for leading the search process to the promising solutions that have a good hydrophobic core and, consequently, improves the efficiency of the whole optimization process. Our differential evolution algorithm was used for demonstrating the efficiency of the two-level optimization. It was analyzed on well-known amino acid sequences that are used frequently in the literature. The obtained experimental results show that the employed two-level optimization improves the efficiency of our algorithm significantly, and that the proposed algorithm is superior to other state-of-the-art algorithms.
Abstract Protein structure prediction is a fundamental issue in the field of computational molecular biology. In this paper, the AB off-lattice model is adopted to transform the original protein structure prediction scheme into a numerical optimization problem. We present a balance-evolution artificial bee colony (BE-ABC) algorithm to address the problem, with the aim of finding the structure for a given protein sequence with the minimal free-energy value. This is achieved through the use of convergence information during the optimization process to adaptively manipulate the search intensity. Besides that, an overall degradation procedure is introduced as part of the BE-ABC algorithm to prevent premature convergence. Comprehensive simulation experiments based on the well-known artificial Fibonacci sequence set and several real sequences from the database of Protein Data Bank have been carried out to compare the performance of BE-ABC against other algorithms. Our numerical results show that the BE-ABC algorithm is able to outperform many state-of-the-art approaches and can be effectively employed for protein structure optimization. Protein folding is a fundamental topic in molecular biology. Conventional experimental techniques for protein structure identification or protein folding recognition require strict laboratory requirements and heavy operating burdens, which have largely limited their applications. Alternatively, computer-aided techniques have been developed to optimize protein structures or to predict the protein folding process. In this paper, we utilize a 3D off-lattice model to describe the original protein folding scheme as a simplified energy-optimal numerical problem, where all types of amino acid residues are binarized into hydrophobic and hydrophilic ones. We apply a balance-evolution artificial bee colony (BE-ABC) algorithm as the minimization solver, which is featured by the adaptive adjustment of search intensity to cater for the varying needs during the entire optimization process. In this work, we establish a benchmark case set with 13 real protein sequences from the Protein Data Bank database and evaluate the convergence performance of BE-ABC algorithm through strict comparisons with several state-of-the-art ABC variants in short-term numerical experiments. Besides that, our obtained best-so-far protein structures are compared to the ones in comprehensive previous literature. This study also provides preliminary insights into how artificial intelligence techniques can be applied to reveal the dynamics of protein folding. Prediction of the three-dimensional structure of a protein from its amino acid sequence can be considered as a global optimization problem. In this paper, the Chaotic Artificial Bee Colony (CABC) algorithm was introduced and applied to 3D protein structure prediction. Based on the 3D off-lattice AB model, the CABC algorithm combines global search and local search of the Artificial Bee Colony (ABC) algorithm with the chaotic search algorithm to avoid the problem of premature convergence and easily trapping the local optimum solution. The experiments carried out with the popular Fibonacci sequences demonstrate that the proposed algorithm provides an effective and high-performance method for protein structure prediction. The biological function of the protein is folded by their spatial structure decisions, and therefore the process of protein folding is one of the most challenging problems in the field of bioinformatics. Although many heuristic algorithms have been proposed to solve the protein structure prediction (PSP) problem. The existing algorithms are far from perfect since PSP is an NP-problem. In this paper, we proposed artificial bee colony algorithm on 3D AB off-lattice model to PSP problem. In order to improve the global convergence ability and convergence speed of ABC algorithm, we adopt the new search strategy by combining the global solution into the search equation. Experimental results illustrate that the suggested algorithm is effective when the algorithm is applied to the Fibonacci sequences and four real protein sequences in the Protein Data Bank.