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266 results for “Protein Modelling”
Micro-anatomic alterations of the placenta in a non-human primate model of gestational protein-restriction
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Supplementary tables S5, S7, S9, S10, original protein models fasta files used for alignments, aligned and manually curated protein modes files used for phylogenies (PHYLIP format), and phylogenetic trees of plant cell wall decomposition gene families from 44 basidiomycete genomes (.tre files)
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Learning protein fitness models from evolutionary and assay-labeled data
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Analytical workflow for "Grad-seq shines light on unrecognized RNA and protein complexes in the model bacterium Escherichia coli", Hör et al. 2020
<p>Analytical workflow including scripts, data and Singularity image for "Grad-seq shines light on unrecognized RNA and protein complexes in the model bacterium Escherichia coli", Hör et al. 2020, (<a href="https://doi.org/10.1101/2020.06.29.177014">https://doi.org/10.1101/2020.06.29.177014</a>)</p>
Supplementary Structural Models (SARS-CoV-2 Spike-RBD:ACE2 complex and TMPRSS2) - SARS-CoV-2 spike protein predicted to form complexes with host receptor protein orthologues from a broad range of mammals
<p>Structural Models (PDB) of SARS-CoV-2 Spike RBD bound to ACE2 receptors of 215 animals.</p> <p>Structural model of Human TMPRSS2.</p> <p>Modelled using the FunMod pipeline and referenced in the preprint</p> <p><a href="https://www.biorxiv.org/content/10.1101/2020.05.01.072371v5">SARS-CoV-2 spike protein predicted to form complexes with host receptor protein orthologues from a broad range of mammals</a></p> <p> </p>
TECPR2 protein models predicted by three algorithms
<p>This ZIP-file contains the files used for TECPR2 protein modeling and resulting PDB (Protein Data Bank) files from three algorithms/pipelines (GalaxyWEB, trRosetta, SWISS-MODEL) used for clustering analysis and visualization in Neuser et al. ("Clinical, neuroimaging and molecular spectrum of <em>TECPR2-</em>associated hereditary sensory and autonomic neuropathy with intellectual disability").<br> We always used standard parameters and the respective top model ("model_1 | model01 | model1") for each algorithm/pipeline and/or downstream steps.</p>
Energy-dependent protein folding: modeling how a protein folding machine may work
<p>MD trajectories of all-atom MD simulations for peptides P1-P5. </p>
Data from: Residue proximity information and protein model discrimination using saturation-suppressor mutagenesis
Identification of residue-residue contacts from primary sequence can be used to guide protein structure prediction. Using Escherichia coli CcdB as the test case, we describe an experimental method termed saturation-suppressor mutagenesis to acquire residue contact information. In this methodology, for each of five inactive CcdB mutants, exhaustive screens for suppressors were performed. Proximal suppressors were accurately discriminated from distal suppressors based on their phenotypes when present as single mutants. Experimentally identified putative proximal pairs formed spatial constraints to recover >98% of native-like models of CcdB from a decoy dataset. Suppressor methodology was also applied to the integral membrane protein, diacylglycerol kinase A where the structures determined by X-ray crystallography and NMR were significantly different. Suppressor as well as sequence co-variation data clearly point to the X-ray structure being the functional one adopted in vivo. The methodology is applicable to any macromolecular system for which a convenient phenotypic assay exists.
Data from: A branch-heterogeneous model of protein evolution for efficient inference of ancestral sequences
Most models of nucleotide or amino acid substitution used in phylogenetic studies assume that the evolutionary process has been homogeneous across lineages and that composition of nucleotides or amino acids has remained the same throughout the tree. These oversimplified assumptions are refuted by the observation that compositional variability characterizes extant biological sequences. Branch-heterogeneous models of protein evolution that account for compositional variability have been developed, but are not yet in common use because of the large number of parameters required, leading to high computational costs and potential overparameterization. Here, we present a new branch-nonhomogeneous and nonstationary model of protein evolution that captures more accurately the high complexity of sequence evolution. This model, henceforth called Correspondence and likelihood analysis (COaLA), makes use of a correspondence analysis to reduce the number of parameters to be optimized through maximum likelihood, focusing on most of the compositional variation observed in the data. The model was thoroughly tested on both simulated and biological data sets to show its high performance in terms of data fitting and CPU time. COaLA efficiently estimates ancestral amino acid frequencies and sequences, making it relevant for studies aiming at reconstructing and resurrecting ancestral amino acid sequences. Finally, we applied COaLA on a concatenate of universal amino acid sequences to confirm previous results obtained with a nonhomogeneous Bayesian model regarding the early pattern of adaptation to optimal growth temperature, supporting the mesophilic nature of the Last Universal Common Ancestor.
Data from: Biophysically inspired model for functionalized nanocarrier adhesion to cell surface: roles of protein expression and mechanical factors
In order to achieve selective targeting of affinity–ligand coated nanoparticles to the target tissue, it is essential to understand the key mechanisms that govern their capture by the target cell. Next-generation pharmacokinetic (PK) models that systematically account for proteomic and mechanical factors can accelerate the design, validation and translation of targeted nanocarriers (NCs) in the clinic. Towards this objective, we have developed a computational model to delineate the roles played by target protein expression and mechanical factors of the target cell membrane in determining the avidity of functionalized NCs to live cells. Model results show quantitative agreement with in vivo experiments when specific and non-specific contributions to NC binding are taken into account. The specific contributions are accounted for through extensive simulations of multivalent receptor–ligand interactions, membrane mechanics and entropic factors such as membrane undulations and receptor translation. The computed NC avidity is strongly dependent on ligand density, receptor expression, bending mechanics of the target cell membrane, as well as entropic factors associated with the membrane and the receptor motion. Our computational model can predict the in vivo targeting levels of the intracellular adhesion molecule-1 (ICAM1)-coated NCs targeted to the lung, heart, kidney, liver and spleen of mouse, when the contributions due to endothelial capture are accounted for. The effect of other cells (such as monocytes, etc.) do not improve the model predictions at steady state. We demonstrate the predictive utility of our model by predicting partitioning coefficients of functionalized NCs in mice and human tissues and report the statistical accuracy of our model predictions under different scenarios.
Data from: Using viromes to predict novel immune proteins in non-model organisms
Immunity is mostly studied in a few model organisms, leaving the majority of immune systems on the planet unexplored. To characterize the immune systems of non-model organisms alternative approaches are required. Viruses manipulate host cell biology through the expression of proteins that modulate the immune response. We hypothesized that metagenomic sequencing of viral communities would be useful to identify both known and unknown host immune proteins. To test this hypothesis, a mock human virome was generated and compared to the human proteome using tBLASTn, resulting in 36 proteins known to be involved in immunity. This same pipeline was then applied to reef-building coral, a non-model organism that currently lacks traditional molecular tools like transgenic animals, gene-editing capabilities, and in vitro cell cultures. Viromes isolated from corals and compared with the predicted coral proteome resulted in 2503 coral proteins, including many proteins involved with pathogen sensing and apoptosis. There were also 159 coral proteins predicted to be involved with coral immunity but currently lacking any functional annotation. The pipeline described here provides a novel method to rapidly predict host immune components that can be applied to virtually any system with the potential to discover novel immune proteins.
SpatPPI: a geometric deep learning model for predicting protein-protein interactions involving intrinsically disordered regions
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DeepGO-SE protein function prediction model data
<p>Data for training and running DeepGO-SE protein function prediction model</p>
Protein expression level dataset (MPB-EXP model dataset)
<p>protein expression level dataset of 88 species</p>
HiPHD: Hierarchical Classification for Protein Remote Homology Detection using Graph Neural Networks and Language Models
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AlphaFold models of protein complexes
<p>AlphaFold models of protein complexes</p>
Conformation Database for Publication: Applying Deep Reinforcement Learning to the HP Model for Protein Structure Prediction
<p><strong>Conformation database</strong> for 2022 Publication "Applying Deep Reinforcement Learning to the HP Model for Protein Structure Prediction"</p> <ul> <li>DOI of Physica A publication: <a href="https://doi.org/10.1016/j.physa.2022.128395">https://doi.org/10.1016/j.physa.2022.128395</a></li> <li>GitHub source code: <a href="https://github.com/CompSoftMatterBiophysics-CityU-HK/Applying-DRL-to-HP-Model-for-Protein-Structure-Prediction">https://github.com/CompSoftMatterBiophysics-CityU-HK/Applying-DRL-to-HP-Model-for-Protein-Structure-Prediction</a></li> </ul> <p>This conformation database shows the distinct conformations of best-known and next best energies:</p> <p>├── <strong>20merA</strong><br> │ ├── <strong>20merA_E8_set</strong><br> │ ├── <strong>20merA_E9_set</strong><br> │ ├── confs_20merA_E8.txt<br> │ └── confs_20merA_E9.txt<br> ├── <strong>20merB</strong><br> │ ├── <strong>20merB_E10_set</strong><br> │ ├── <strong>20merB_E9_set</strong><br> │ ├── confs_20merB_E10.txt<br> │ └── confs_20merB_E9.txt<br> ├── <strong>24mer</strong><br> │ ├── <strong>24mer_E8_set</strong><br> │ ├── <strong>24mer_E9_set</strong><br> │ ├── confs_24mer_E8.txt<br> │ └── confs_24mer_E9.txt<br> ├── <strong>25mer</strong><br> │ ├── <strong>25mer_E7_set</strong><br> │ ├── <strong>25mer_E8_set</strong><br> │ ├── confs_25mer_E7.txt<br> │ └── confs_25mer_E8.txt<br> ├── <strong>36mer</strong><br> │ ├── <strong>36mer_E13_set</strong><br> │ ├── <strong>36mer_E14_set</strong><br> │ ├── confs_36mer_E13.txt<br> │ └── confs_36mer_E14.txt<br> ├── <strong>48mer</strong><br> │ ├── <strong>48mer_E22_set</strong><br> │ ├── <strong>48mer_E23_set</strong><br> │ ├── confs_48mer_E22.txt<br> │ └── confs_48mer_E23.txt<br> └── <strong>50mer</strong><br> ├── <strong>50mer_E20_set</strong><br> ├── <strong>50mer_E21_set</strong><br> ├── confs_50mer_E20.txt<br> └── confs_50mer_E21.txt</p>
CATH-KinFams: CATH Protein Kinase classification alignments and Hidden Markov Models
<p>CATH KinFams are protein kinase domain families classified according to functional similarity based on SDP. In this deposition we make available 2,210 KinFams sequence alignments alongside Hidden Markov Models built from them to be used with HMMER3.</p> <p>A concatenated library 'kinases_4.3-FF-seed.hmm' is also available to scan against the whole KinFams dataset.</p> <p>The Zenodo deposition contains:</p> <p>kinfams-cath-4.3-seed-alignments.tar.gz - KinFams FASTA file alignments with headers 'UniProt_ID/start-stop' i.e. A8XMX4/281-587</p> <p>kinfams-cath-4.3-seed-hmms.tar.gz - HMMs for each individual KinFam and concatenated in a HMM library.</p> <p>kinfams-cath-4.3-seed-mda-strings - Multi-Domain-Architecture string assignment for each sequence in the KinFams dataset.</p> <p>human_kinfams_af2_models_cif.tar.gz - Chopped mmCIF files containing Human Kinases AlphaFold2 Models.</p>
Astrocytic Expression of Yes-Associated Protein (YAP) Regu-lates Retinal Neovascularization in a Mouse Model of Oxy-gen-Induced Retinopathy
<p>Original images used for each figure.</p>
Stepwise design of pseudosymmetric protein hetero-oligomers; design models
<p>Design models for the associated publication</p>
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Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.
DANDI Archive for NWB datasets
DANDI is a BRAIN Initiative archive for publishing and sharing neurophysiology data, including electrophysiology, optophysiology, and behavioral data packaged as NWB and related standards.
International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.