A multi-objective evolutionary approach to the protein structure prediction problem.
Ontology highlight
ABSTRACT:
SUBMITTER: Cutello V
PROVIDER: S-EPMC1629082 | biostudies-literature | 2006 Feb
REPOSITORIES: biostudies-literature
Publications
A multi-objective evolutionary approach to the protein structure prediction problem.
Cutello Vincenzo V Narzisi Giuseppe G Nicosia Giuseppe G
Journal of the Royal Society, Interface 20060201 6
The protein structure prediction (PSP) problem is concerned with the prediction of the folded, native, tertiary structure of a protein given its sequence of amino acids. It is a challenging and computationally open problem, as proven by the numerous methodological attempts and the research effort applied to it in the last few years. The potential energy functions used in the literature to evaluate the conformation of a protein are based on the calculations of two different interaction energies: ...[more]
Similar Datasets
Project description:BACKGROUND: Elucidating the native structure of a protein molecule from its sequence of amino acids, a problem known as de novo structure prediction, is a long standing challenge in computational structural biology. Difficulties in silico arise due to the high dimensionality of the protein conformational space and the ruggedness of the associated energy surface. The issue of multiple minima is a particularly troublesome hallmark of energy surfaces probed with current energy functions. In contrast to the true energy surface, these surfaces are weakly-funneled and rich in comparably deep minima populated by non-native structures. For this reason, many algorithms seek to be inclusive and obtain a broad view of the low-energy regions through an ensemble of low-energy (decoy) conformations. Conformational diversity in this ensemble is key to increasing the likelihood that the native structure has been captured. METHODS: We propose an evolutionary search approach to address the multiple-minima problem in decoy sampling for de novo structure prediction. Two population-based evolutionary search algorithms are presented that follow the basic approach of treating conformations as individuals in an evolving population. Coarse graining and molecular fragment replacement are used to efficiently obtain protein-like child conformations from parents. Potential energy is used both to bias parent selection and determine which subset of parents and children will be retained in the evolving population. The effect on the decoy ensemble of sampling minima directly is measured by additionally mapping a conformation to its nearest local minimum before considering it for retainment. The resulting memetic algorithm thus evolves not just a population of conformations but a population of local minima. RESULTS AND CONCLUSIONS: Results show that both algorithms are effective in terms of sampling conformations in proximity of the known native structure. The additional minimization is shown to be key to enhancing sampling capability and obtaining a diverse ensemble of decoy conformations, circumventing premature convergence to sub-optimal regions in the conformational space, and approaching the native structure with proximity that is comparable to state-of-the-art decoy sampling methods. The results are shown to be robust and valid when using two representative state-of-the-art coarse-grained energy functions.
| S-EPMC3953177 | biostudies-literature
Project description:Protein structure prediction (PSP) is concerned with the prediction of protein tertiary structure from primary structure and is a challenging calculation problem. After decades of research effort, numerous solutions have been proposed for optimisation methods based on energy models. However, further investigation and improvement is still needed to increase the accuracy and similarity of structures. This study presents a novel backbone angle preference factor, which is one of the factors inducing protein folding. The proposed multiobjective optimisation approach simultaneously considers energy models and backbone angle preferences to solve the ab initio PSP. To prove the effectiveness of the multiobjective optimisation approach based on the energy models and backbone angle preferences, 75 amino acid sequences with lengths ranging from 22 to 88 amino acids were selected from the CB513 data set to be the benchmarks. The data sets were highly dissimilar, therefore indicating that they are meaningful. The experimental results showed that the root-mean-square deviation (RMSD) of the multiobjective optimization approach based on energy model and backbone angle preferences was superior to those of typical energy models, indicating that the proposed approach can facilitate the ab initio PSP.
| S-EPMC4519891 | biostudies-literature
Project description:When researchers complete a manuscript, they need to choose a journal to which they will submit the study. This decision requires to navigate trade-offs between multiple objectives. One objective is to share the new knowledge as widely as possible. Citation counts can serve as a proxy to quantify this objective. A second objective is to minimize the time commitment put into sharing the research, which may be estimated by the total time from initial submission to final decision. A third objective is to minimize the number of rejections and resubmissions. Thus, researchers often consider the trade-offs between the objectives of (i) maximizing citations, (ii) minimizing time-to-decision, and (iii) minimizing the number of resubmissions. To complicate matters further, this is a decision with multiple, potentially conflicting, decision-maker rationalities. Co-authors might have different preferences, for example about publishing fast versus maximizing citations. These diverging preferences can lead to conflicting trade-offs between objectives. Here, we apply a multi-objective decision analytical framework to identify the Pareto-front between these objectives and determine the set of journal submission pathways that balance these objectives for three stages of a researcher's career. We find multiple strategies that researchers might pursue, depending on how they value minimizing risk and effort relative to maximizing citations. The sequences that maximize expected citations within each strategy are generally similar, regardless of time horizon. We find that the "conditional impact factor"-impact factor times acceptance rate-is a suitable heuristic method for ranking journals, to strike a balance between minimizing effort objectives and maximizing citation count. Finally, we examine potential co-author tension resulting from differing rationalities by mapping out each researcher's preferred Pareto front and identifying compromise submission strategies. The explicit representation of trade-offs, especially when multiple decision-makers (co-authors) have different preferences, facilitates negotiations and can support the decision process.
| S-EPMC5459441 | biostudies-literature
Project description:Given a protein sequence and a number of potential domains matching it, what are the domain content and the most likely domain architecture for the sequence? This problem is of fundamental importance in protein annotation, constituting one of the main steps of all predictive annotation strategies. On the other hand, when potential domains are several and in conflict because of overlapping domain boundaries, finding a solution for the problem might become difficult. An accurate prediction of the domain architecture of a multi-domain protein provides important information for function prediction, comparative genomics and molecular evolution.We developed DAMA (Domain Annotation by a Multi-objective Approach), a novel approach that identifies architectures through a multi-objective optimization algorithm combining scores of domain matches, previously observed multi-domain co-occurrence and domain overlapping. DAMA has been validated on a known benchmark dataset based on CATH structural domain assignments and on the set of Plasmodium falciparum proteins. When compared with existing tools on both datasets, it outperforms all of them.DAMA software is implemented in C++ and the source code can be found at http://www.lcqb.upmc.fr/DAMA.juliana.silva_bernardes@upmc.fr or alessandra.carbone@lip6.frSupplementary data are available at Bioinformatics online.
| S-EPMC4734041 | biostudies-literature
Project description:MotivationProtein structure refinement is an important step of protein structure prediction. Existing approaches have generally used a single scoring function combined with Monte Carlo method or Molecular Dynamics algorithm. The one-dimension optimization of a single energy function may take the structure too far away without a constraint. The basic motivation of our study is to reduce the bias problem caused by minimizing only a single energy function due to the very diversity of different protein structures.ResultsWe report a new Artificial Intelligence-based protein structure Refinement method called AIR. Its fundamental idea is to use multiple energy functions as multi-objectives in an effort to correct the potential inaccuracy from a single function. A multi-objective particle swarm optimization algorithm-based structure refinement is designed, where each structure is considered as a particle in the protocol. With the refinement iterations, the particles move around. The quality of particles in each iteration is evaluated by three energy functions, and the non-dominated particles are put into a set called Pareto set. After enough iteration times, particles from the Pareto set are screened and part of the top solutions are outputted as the final refined structures. The multi-objective energy function optimization strategy designed in the AIR protocol provides a different constraint view of the structure, by extending the one-dimension optimization to a new three-dimension space optimization driven by the multi-objective particle swarm optimization engine. Experimental results on CASP11, CASP12 refinement targets and blind tests in CASP 13 turn to be promising.Availability and implementationThe AIR is available online at: www.csbio.sjtu.edu.cn/bioinf/AIR/.Supplementary informationSupplementary data are available at Bioinformatics online.
| S-EPMC7999140 | biostudies-literature
Project description:OBJECTIVES:To predict the structure of protein, which dictates the function it performs, a newly designed algorithm is developed which blends the concept of self-organization and the genetic algorithm. METHODS:Among many other approaches, genetic algorithm is found to be a promising cooperative computational method to solve protein structure prediction in a reasonable time. To automate the right choice of parameter values the influence of self-organization is adopted to design a new genetic operator to optimize the process of prediction. Torsion angles, the local structural parameters which define the backbone of protein are considered to encode the chromosome that enhances the quality of the confirmation. Newly designed self-configured genetic operators are used to develop self-organizing genetic algorithm to facilitate the accurate structure prediction. RESULTS:Peptides are used to gauge the validity of the proposed algorithm. As a result, the structure predicted shows clear improvements in the root mean square deviation on overlapping the native indicates the overall performance of the algorithm. In addition, the Ramachandran plot results implies that the conformations of phi-psi angles in the predicted structure are better as compared to native and also free from steric hindrances. CONCLUSIONS:The proposed algorithm is promising which contributes to the prediction of a native-like structure by eliminating the time constraint and effort demand. In addition, the energy of the predicted structure is minimized to a greater extent, which proves the stability of protein.
| S-EPMC3717437 | biostudies-literature
Project description:For naturally occurring proteins, similar sequence implies similar structure. Consequently, multiple sequence alignments (MSAs) often are used in template-based modeling of protein structure and have been incorporated into fragment-based assembly methods. Our previous homology-free structure prediction study introduced an algorithm that mimics the folding pathway by coupling the formation of secondary and tertiary structure. Moves in the Monte Carlo procedure involve only a change in a single pair of phi,psi backbone dihedral angles that are obtained from a Protein Data Bank-based distribution appropriate for each amino acid, conditional on the type and conformation of the flanking residues. We improve this method by using MSAs to enrich the sampling distribution, but in a manner that does not require structural knowledge of any protein sequence (i.e., not homologous fragment insertion). In combination with other tools, including clustering and refinement, the accuracies of the predicted secondary and tertiary structures are substantially improved and a global and position-resolved measure of confidence is introduced for the accuracy of the predictions. Performance of the method in the Critical Assessment of Structure Prediction (CASP8) is discussed.
| S-EPMC2866277 | biostudies-literature
Project description:Data classification is a fundamental task in data mining. Within this field, the classification of multi-labeled data has been seriously considered in recent years. In such problems, each data entity can simultaneously belong to several categories. Multi-label classification is important because of many recent real-world applications in which each entity has more than one label. To improve the performance of multi-label classification, feature selection plays an important role. It involves identifying and removing irrelevant and redundant features that unnecessarily increase the dimensions of the search space for the classification problems. However, classification may fail with an extreme decrease in the number of relevant features. Thus, minimizing the number of features and maximizing the classification accuracy are two desirable but conflicting objectives in multi-label feature selection. In this article, we introduce a multi-objective optimization algorithm customized for selecting the features of multi-label data. The proposed algorithm is an enhanced variant of a decomposition-based multi-objective optimization approach, in which the multi-label feature selection problem is divided into single-objective subproblems that can be simultaneously solved using an evolutionary algorithm. This approach leads to accelerating the optimization process and finding more diverse feature subsets. The proposed method benefits from a local search operator to find better solutions for each subproblem. We also define a pool of genetic operators to generate new feature subsets based on old generation. To evaluate the performance of the proposed algorithm, we compare it with two other multi-objective feature selection approaches on eight real-world benchmark datasets that are commonly used for multi-label classification. The reported results of multi-objective method evaluation measures, such as hypervolume indicator and set coverage, illustrate an improvement in the results obtained by the proposed method. Moreover, the proposed method achieved better results in terms of classification accuracy with fewer features compared with state-of-the-art methods.
| S-EPMC7924502 | biostudies-literature
Project description:We describe our global optimization method called Stochastic Perturbation with Soft Constraints (SPSC), which uses information from known proteins to predict secondary structure, but not in the tertiary structure predictions or in generating the terms of the physics-based energy function. Our approach is also characterized by the use of an all atom energy function that includes a novel hydrophobic solvation function derived from experiments that shows promising ability for energy discrimination against misfolded structures. We present the results obtained using our SPSC method and energy function for blind prediction in the 4th Critical Assessment of Techniques for Protein Structure Prediction competition, and show that our approach is more effective on targets for which less information from known proteins is available. In fact our SPSC method produced the best prediction for one of the most difficult targets of the competition, a new fold protein of 240 amino acids.
| S-EPMC1302447 | biostudies-other
Project description:The design and construction of network structures oriented towards different applications has attracted much attention recently. The existing studies indicated that structural heterogeneity plays different roles in promoting cooperation and robustness. Compared with rewiring a predefined network, it is more flexible and practical to construct new networks that satisfy the desired properties. Therefore, in this paper, we study a method for constructing robust cooperative networks where the only constraint is that the number of nodes and links is predefined. We model this network construction problem as a multi-objective optimization problem and propose a multi-objective evolutionary algorithm, named MOEA-Netrc, to generate the desired networks from arbitrary initializations. The performance of MOEA-Netrc is validated on several synthetic and real-world networks. The results show that MOEA-Netrc can construct balanced candidates and is insensitive to the initializations. MOEA-Netrc can find the Pareto fronts for networks with different levels of cooperation and robustness. In addition, further investigation of the robustness of the constructed networks revealed the impact on other aspects of robustness during the construction process.
| S-EPMC5278550 | biostudies-literature