CoMOGrad and PHOG: From Computer Vision to Fast and Accurate Protein Tertiary Structure Retrieval.
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ABSTRACT:
SUBMITTER: Karim R
PROVIDER: S-EPMC4543952 | biostudies-literature |
REPOSITORIES: biostudies-literature
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Project description:BACKGROUND: In recent times, there has been an exponential rise in the number of protein structures in databases e.g. PDB. So, design of fast algorithms capable of querying such databases is becoming an increasingly important research issue. This paper reports an algorithm, motivated from spectral graph matching techniques, for retrieving protein structures similar to a query structure from a large protein structure database. Each protein structure is specified by the 3D coordinates of residues of the protein. The algorithm is based on a novel characterization of the residues, called projections, leading to a similarity measure between the residues of the two proteins. This measure is exploited to efficiently compute the optimal equivalences. RESULTS: Experimental results show that, the current algorithm outperforms the state of the art on benchmark datasets in terms of speed without losing accuracy. Search results on SCOP 95% nonredundant database, for fold similarity with 5 proteins from different SCOP classes show that the current method performs competitively with the standard algorithm CE. The algorithm is also capable of detecting non-topological similarities between two proteins which is not possible with most of the state of the art tools like Dali.
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Project description:Landmark-based geometric morphometrics has emerged as an essential discipline for the quantitative analysis of size and shape in ecology and evolution. With the ever-increasing density of digitized landmarks, the possible development of a fully automated method of landmark placement has attracted considerable attention. Despite the recent progress in image registration techniques, which could provide a pathway to automation, three-dimensional (3D) morphometric data are still mainly gathered by trained experts. For the most part, the large infrastructure requirements necessary to perform image-based registration, together with its system specificity and its overall speed, have prevented its wide dissemination.Here, we propose and implement a general and lightweight point cloud-based approach to automatically collect high-dimensional landmark data in 3D surfaces (Automated Landmarking through Point cloud Alignment and Correspondence Analysis). Our framework possesses several advantages compared with image-based approaches. First, it presents comparable landmarking accuracy, despite relying on a single, random reference specimen and much sparser sampling of the structure's surface. Second, it can be efficiently run on consumer-grade personal computers. Finally, it is general and can be applied at the intraspecific level to any biological structure of interest, regardless of whether anatomical atlases are available.Our validation procedures indicate that the method can recover intraspecific patterns of morphological variation that are largely comparable to those obtained by manual digitization, indicating that the use of an automated landmarking approach should not result in different conclusions regarding the nature of multivariate patterns of morphological variation.The proposed point cloud-based approach has the potential to increase the scale and reproducibility of morphometrics research. To allow ALPACA to be used out-of-the-box by users with no prior programming experience, we implemented it as a SlicerMorph module. SlicerMorph is an extension that enables geometric morphometrics data collection and 3D specimen analysis within the open-source 3D Slicer biomedical visualization ecosystem. We expect that convenient access to this platform will make ALPACA broadly applicable within ecology and evolution.
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Project description:As structure prediction methods are generating millions of publicly available protein structures, searching these databases is becoming a bottleneck. Foldseek aligns the structure of a query protein against a database by describing tertiary amino acid interactions within proteins as sequences over a structural alphabet. Foldseek decreases computation times by four to five orders of magnitude with 86%, 88% and 133% of the sensitivities of Dali, TM-align and CE, respectively.
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Project description:Given the close relationship between protein structure and function, protein structure searches have long played an established role in bioinformatics. Despite their maturity, existing protein structure searches either use simplifying assumptions or compromise between fast response times and quality of results. These limitations can prevent the easy and efficient exploration of relationships between protein structures, which is the norm in other areas of inquiry. To address these limitations we have developed RUPEE, a fast and accurate purely geometric structure search combining techniques from information retrieval and big data with a novel approach to encoding sequences of torsion angles. Comparing our results to the output of mTM, SSM, and the CATHEDRAL structural scan, it is clear that RUPEE has set a new bar for purely geometric big data approaches to protein structure searches. RUPEE in top-aligned mode produces equal or better results than the best available protein structure searches, and RUPEE in fast mode demonstrates the fastest response times coupled with high quality results. The RUPEE protein structure search is available at https://ayoubresearch.com. Code and data are available at https://github.com/rayoub/rupee.
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Project description:Mankind directly controls the environment and lifestyles of several domestic species for purposes ranging from production and research to conservation and companionship. These environments and lifestyles may not offer these animals the best quality of life. Behaviour is a direct reflection of how the animal is coping with its environment. Behavioural indicators are thus among the preferred parameters to assess welfare. However, behavioural recording (usually from video) can be very time consuming and the accuracy and reliability of the output rely on the experience and background of the observers. The outburst of new video technology and computer image processing gives the basis for promising solutions. In this pilot study, we present a new prototype software able to automatically infer the behaviour of dogs housed in kennels from 3D visual data and through structured machine learning frameworks. Depth information acquired through 3D features, body part detection and training are the key elements that allow the machine to recognise postures, trajectories inside the kennel and patterns of movement that can be later labelled at convenience. The main innovation of the software is its ability to automatically cluster frequently observed temporal patterns of movement without any pre-set ethogram. Conversely, when common patterns are defined through training, a deviation from normal behaviour in time or between individuals could be assessed. The software accuracy in correctly detecting the dogs' behaviour was checked through a validation process. An automatic behaviour recognition system, independent from human subjectivity, could add scientific knowledge on animals' quality of life in confinement as well as saving time and resources. This 3D framework was designed to be invariant to the dog's shape and size and could be extended to farm, laboratory and zoo quadrupeds in artificial housing. The computer vision technique applied to this software is innovative in non-human animal behaviour science. Further improvements and validation are needed, and future applications and limitations are discussed.
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Project description:QSCOP is a quantitative structural classification of proteins which distinguishes itself from other classifications by two essential properties: (i) QSCOP is concurrent with the Research Collaboratory for Structural Bioinformatics (RCSB) Protein Data Bank and (ii) QSCOP covers the widely used SCOP classification with layers of quantitative structural information. The QSCOP-BLAST web server presented here combines the BLAST sequence search engine with QSCOP to retrieve, for a given query sequence, all structural information currently available. The resulting search engine is reliable in terms of the quality of results obtained, and it is efficient in that results are displayed instantaneously. The hierarchical organization of QSCOP is used to control the redundancy and diversity of the retrieved hits with the benefit that the often cumbersome and difficult interpretation of search results is an intuitive and straightforward exercise. We demonstrate the use of QSCOP-BLAST by example. The server is accessible at http://qscop-blast.services.came.sbg.ac.at/
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Project description:Motivation:As protein structure is more conserved than sequence during evolution, multiple structure alignment can be more informative than multiple sequence alignment, especially for distantly related proteins. With the rapid increase of the number of protein structures in the Protein Data Bank, it becomes urgent to develop efficient algorithms for multiple structure alignment. Results:A new multiple structure alignment algorithm (mTM-align) was proposed, which is an extension of the highly efficient pairwise structure alignment program TM-align. The algorithm was benchmarked on four widely used datasets, HOMSTRAD, SABmark_sup, SABmark_twi and SISY-multiple, showing that mTM-align consistently outperforms other algorithms. In addition, the comparison with the manually curated alignments in the HOMSTRAD database shows that the automated alignments built by mTM-align are in general more accurate. Therefore, mTM-align may be used as a reliable complement to construct multiple structure alignments for real-world applications. Availability and implementation:http://yanglab.nankai.edu.cn/mTM-align. Contact:zhng@umich.edu or yangjy@nankai.edu.cn. Supplementary information:Supplementary data are available at Bioinformatics online.
| S-EPMC5946935 | biostudies-literature
Project description:BackgroundStudying the functions and structures of proteins is important for understanding the molecular mechanisms of life. The number of publicly available protein structures has increasingly become extremely large. Still, the classification of a protein structure remains a difficult, costly, and time consuming task. The difficulties are often due to the essential role of spatial and topological structures in the classification of protein structures.ResultsWe propose ProtNN, a novel classification approach for protein 3D-structures. Given an unannotated query protein structure and a set of annotated proteins, ProtNN assigns to the query protein the class with the highest number of votes across the k nearest neighbor reference proteins, where k is a user-defined parameter. The search of the nearest neighbor annotated structures is based on a protein-graph representation model and pairwise similarities between vector embedding of the query and the reference protein structures in structural and topological spaces.ConclusionsWe demonstrate through an extensive experimental evaluation that ProtNN is able to accurately classify several datasets in an extremely fast runtime compared to state-of-the-art approaches. We further show that ProtNN is able to scale up to a whole PDB dataset in a single-process mode with no parallelization, with a gain of thousands order of magnitude in runtime compared to state-of-the-art approaches.
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Project description:PurposeWe propose a fast, patient-specific workflow for on-line specific absorption rate (SAR) supervision. An individualized electromagnetic model is created while the subject is on the table, followed by rapid SAR estimates for that individual. Our goal is an improved correspondence between the patient and model, reducing reliance on general anatomical body models.MethodsA 3D fat-water 3T acquisition (~2 minutes) is automatically segmented using a computer vision algorithm (~1 minute) into what we found to be the most important electromagnetic tissue classes: air, bone, fat, and soft tissues. We then compute the individual's EM field exposure and global and local SAR matrices using a fast electromagnetic integral equation solver. We assess the approach in 10 volunteers and compare to the SAR seen in a standard generic body model (Duke).ResultsThe on-the-table workflow averaged 7'44″. Simulation of the simplified Duke models confirmed that only air, bone, fat, and soft tissue classes are needed to estimate global and local SAR with an error of 6.7% and 2.7%, respectively, compared to the full model. In contrast, our volunteers showed a 16.0% and 20.3% population variability in global and local SAR, respectively, which was mostly underestimated by the Duke model.ConclusionTimely construction and deployment of a patient-specific model is computationally feasible. The benefit of resolving the population heterogeneity compared favorably to the modest modeling error incurred. This suggests that individualized SAR estimates can improve electromagnetic safety in MRI and possibly reduce conservative safety margins that account for patient-model mismatch, especially in non-standard patients.
| S-EPMC7722143 | biostudies-literature
Project description:MotivationThe investigation of the structure of biological systems at the molecular level gives insights about their functions and dynamics. Shape and surface of biomolecules are fundamental to molecular recognition events. Characterizing their geometry can lead to more adequate predictions of their interactions. In the present work, we assess the performance of reference shape retrieval methods from the computer vision community on protein shapes.ResultsShape retrieval methods are efficient in identifying orthologous proteins and tracking large conformational changes. This work illustrates the interest for the protein surface shape as a higher-level representation of the protein structure that (i) abstracts the underlying protein sequence, structure or fold, (ii) allows the use of shape retrieval methods to screen large databases of protein structures to identify surficial homologs and possible interacting partners and (iii) opens an extension of the protein structure-function paradigm toward a protein structure-surface(s)-function paradigm.Availabilityand implementationAll data are available online at http://datasetmachat.drugdesign.fr.Supplementary informationSupplementary data are available at Bioinformatics online.
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