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219 results for “protein dynamics”
Data from: Physics-informed deep learning for plasmonic sensing of nanoscale protein dynamics in solution
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Molecular dynamics simulations of intrinsically disordered proteins p53TAD and Pup
Open the record for dataset details and reuse information.
Data for "Nanosecond Protein Dynamics in a Red/Green Cyanobacteriochrome Revealed by Transient IR Spectroscopy "
<p>Raw data behind manuscript figures.</p>
Phospho-seq: Integrated, multi-modal profiling of intracellular protein dynamics in single cells
<p> </p><p>Datasets to go along with the publication listed:</p><p>full_object.rds: Brain Organoid Phospho-Seq dataset with ATAC, Protein and imputed RNA data</p><p>rna_object.rds: Reference whole cell scRNA-Seq object on Brain organoids</p><p>multiome_object.rds: Bridge dataset containing RNA and ATAC modalities for Brain organoids</p><p>metacell_allnorm.rds: Metacell object for finding gene-peak-protein linkages in Brain organoid dataset</p><p>fullobject_fragments.tsv.gz: fragment file to go with the full object</p><p>fullobject_fragments.tsv.gz.tbi:index file for the full object fragment file</p><p>multiome_fragments.tsv.gz: fragment file to go with the multiome object</p><p>multiome_fragments.tsv.gz.tbi:index file for the multiome object fragment file</p><p>K562_Stem.rds : object corresponding to the pilot experiment including K562 cells and iPS cells</p><p>K562_stem_fragments.tsv.gz: fragment file to go with the K562_stem object</p><p>K562_stem_fragments.tsv.gz.tbi: index file for the K562_stem object fragment file</p><p>retina.rds : object corresponding to the retinal organoid phospho-seq experiment</p><p>retina_fragments.tsv.gz: fragment file to go with the retina object</p><p>retina_fragments.tsv.gz.tbi: index file for the retina object fragment file</p><p>retina_multi.rds : object corresponding to the retinal organoid phospho-seq-multiome experiment</p><p>retina_multi_fragments.tsv.gz: fragment file to go with the retina_multi object</p><p>retina_multi_fragments.tsv.gz.tbi: index file for the retina_multi object fragment file</p><p>To use the K562, multiome, retina and retina_multiome datasets provided, please use these lines of code to import the object into Signac/Seurat and change the fragment file path to the corresponding downloaded fragment file:</p><p>obj <- readRDS("obj.rds") # remove fragment file information Fragments(obj) <- NULL # Update the path of the fragment file Fragments(obj) <- CreateFragmentObject(path = "download/obj_fragments.tsv.gz", cells = Cells(obj))</p><p>To use the K562 and multiome datasets provided, please use these lines of code to import the object into Signac/Seurat and change the fragment file path to the corresponding downloaded fragment file:</p><p>obj <- readRDS("obj.rds") # remove fragment file information Fragments(obj) <- NULL # Update the path of the fragment file Fragments(obj) <- CreateFragmentObject(path = "download/obj_fragments.tsv.gz", cells = Cells(obj))</p><p>To use the "fullobject" dataset provided, please use these lines of code to import the object into Signac/Seurat and change the fragment file path to the corresponding downloaded fragment file: </p><p>#load the stringr package library(stringr) #load the object obj <- readRDS("obj.rds") # remove fragment file information Fragments(obj) <- NULL #Remove unwanted residual information and rename cells obj@reductions$norm.adt.pca <- NULL obj@reductions$norm.pca <- NULL obj <- RenameCells(obj, new.names = str_remove(Cells(obj), "atac_")) # Update the path of the fragment file Fragments(obj) <- CreateFragmentObject(path = "download/obj_fragments.tsv.gz", cells = Cells(obj))</p><p> </p><p> </p>
Photoactivation of the Orange Carotenoid Protein Requires Two Light-Driven Reactions Mediated by a Metastable Monomeric Intermediate – Absorption Spectra and Global Analysis Results, Molecular Dynamics Simulations
<p>Time-resolved absorption and molecular dynamics trajectory datasets associated with: Rose, J. B.; Gascón, J. A.; Sutter, M.; Sheppard, D. I.; Kerfeld, C. A.; Beck, W. F. Photoactivation of the Orange Carotenoid Protein Requires Two Light-Driven Reactions Mediated by a Metastable Monomeric Intermediate. <i>Phys. Chem. Chem. Phys.</i> <strong>2023</strong>, DOI: 10.1039/d3cp04484j.</p>
Single cell imaging of ERK and Akt activation dynamics and heterogeneity induced by G protein-coupled receptors - Scripts & Source data
<p>Source data and scripts to reproduce the figures that are part of the publication "Single cell imaging of ERK and Akt activation dynamics and heterogeneity induced by G protein-coupled receptors".</p> <p>Journal of Cell Science (2022) 135, jcs259685, DOI: 10.1242/jcs.259685</p> <p> </p> <p>An earlier version of this work is published as a preprint: "Heterogeneity and dynamics of ERK and Akt activation by G protein-coupled receptors depend on the activated heterotrimeric G proteins", DOI: <a href="https://doi.org/10.1101/2021.07.27.453948">10.1101/2021.07.27.453948</a></p>
Statin therapy inhibits fatty acid synthase via dynamic protein modifications
<p>Statins are a class of drugs widely prescribed to prevent cardiovascular disease, with pleiotropic cellular effects. Statins inhibit HMG-CoA reductase (HMGCR), which converts the metabolite HMG-CoA into mevalonate. Recent discoveries revealed HMG-CoA is a reactive metabolite that can non-enzymatically modify proteins and impact their activity. Therefore, we predicted that inhibition of HMGCR by statins might increase HMG-CoA levels and protein modifications. We observed a substantial increase in HMG-CoA levels upon statin treatment, and only a single protein was modified. Mass spectrometry revealed fatty acid synthase (FAS) was modified on active site residues, and surprisingly, the modification is located on non-lysine side-chains. The dynamic modifications occur only on a sub-pool of FAS near HMGCR and alter cellular signaling around the ER and Golgi. These results uncover communication between cholesterol and lipid biosynthesis by the substrate of one pathway inhibiting another in a rapid and reversible manner. </p>
Molecular dynamics trajectories of protein folding
<p>Molecular dynamics trajectories of protein folding are deposited for educational purposes.</p> <p>Currently, the following trajectories are available:</p> <ul> <li>Chignolin (five independent NVT simulations up to 1.5 micro-sec): <ul> <li>`movie.pse` is a PyMOL session file of MD trajectories. </li> <li>`movie.mp4` is a movie file that shows you how a protein folds during simulation.</li> <li>xtc files (Gromacs compressed format) and corresponding tpr files.</li> <li>gro files for movie making</li> </ul> </li> </ul> <p> </p> <p>Computational setting </p> <ul> <li>Amber ff99SB-ILDN for protein (Lindorff-Larsen, K. <em>et al.</em> Improved side-chain torsion potentials for the Amber ff99SB protein force field. <em>Proteins</em> <strong>78</strong>, 1950–1958 (2010))</li> <li>TIP3P water model</li> <li>0.1 M salt concentration </li> <li>NVT ensemble at 300 K with V-rescale thermostat (Bussi, G., Donadio, D. & Parrinello, M. Canonical sampling through velocity rescaling. <em>J. Chem. Phys.</em> <strong>126</strong>, 014101 (2007))</li> <li>Time step : 2 fs</li> <li>gromacs-2020.6</li> </ul>
Insights into the stability of engineered mini-proteins from their dynamic electronic properties
<p>Coordinates and partial charges from GFN2-xTB and wPBEh/cc-pvdz for 20 ps x 20 replicas for two variants of Trp-cage (TC5b and TC10b) as supporting information.</p>
Chanalyzer: a computational geometry approach for the analysis of protein channel shape and dynamics
<p>Dataset of molecular dynamics trajectories described in the "Chanalyzer: a computational geometry approach for the analysis of protein channel shape and dynamics" work.</p> <p>Trajectories of differently functionalized MscL channel forms. </p> <p>The *_xyzr.tar.gz files contain the processed frames in the xyzr format, which is a compatible input for NanoShaper</p> <p>The conf.prm file is the parameter file that has been used for the NanoShaper tool</p>
Code and Data for "Real-time dynamic single-molecule protein sequencing on an integrated semiconductor device"
<p><strong>Code and Data for "Real-time dynamic single-molecule protein sequencing on an integrated semiconductor device".</strong></p> <pre>Code to analyze data produced by the Quantum-Si benchtop device and semiconductor chip is provided in a Python library <strong>qsi_algo</strong> under several submodules: - <strong>rs_caller.py</strong>: Algorithm for calling RS segments (also called ROI segments throughout code). - <strong>rs_caller_controller.py</strong>: Code framework for executing RS calling and property computation in a distributed manner - <strong>rs_properties</strong>: Code for computing properties of identified RS - <strong>rs_classifier</strong>: Algorithms for identifying peptide states (i.e. residue calls) associated with an RS - <strong>utils.py</strong>: shared helper code - <strong>pulse_reader</strong>: reader for binary pulse file - <strong>filters</strong>: ROI and pulse filtering utilities - <strong>plotting</strong>: functions for visualization of data relevant to the analyses presented Jupyter notebooks (<strong>.ipynb</strong>) files are named according to the manuscript figure they are associated with. Analysis code inside uses provided RS (recognition segment) data to demonstrate filtering and residue-calling techniques required to replicate analyses shown in manuscript figures. Please note: several methods rely on randomization for model initialization and/or data sampling which can cause small deviations from equivalent analyses in published figures. The raw data produced from the Quantum-Si benchtop device and semiconductor chip for the assays presented in the accompanying study is presented in a pulse-called binary file format. Pulses can be used as input for RS identification and peptide state identification. Pre-segmented (RS-identified) files are included for convenience. The data contained in the files include: <strong>{run_id}.bin</strong>: Binary format for storing pulse info. The reader provided in <strong>qsi_algo.pulse_reader</strong> produces the following columns: - <strong>aperture_index</strong>: unique aperture index on chip - <strong>start_f</strong>: index of first frame in pulse, counted from the beginning of the run - <strong>end_f</strong>: index of last frame in pulse, counted from the beginning of the run - <strong>dur_f</strong>: duration of pulse in frames - <strong>dur_s</strong>: duration of pulse in seconds - <strong>ipd_f</strong>: interpulse duration in frames (number of frames since end of preceding pulse) - <strong>ipd_s</strong>: interpulse duration in seconds (time in seconds elapsed since end of preceding pulse) - <strong>snr</strong>: signal-to-noise ratio (bin1_intensity / bin1_bg_std) - <strong>intensity</strong>: intensity of pulse (counts above baseline in bin1) - <strong>bin0_intensity</strong>: counts above baseline in bin0 - <strong>intensity_display</strong>: bin1_intensity + bin1_bg_mean - <strong>binratio</strong>: bin0_intensity / bin1_intensity - <strong>bg_mean</strong>: bin1 background mean in region of pulse - <strong>bg_std</strong>: bin1 background standard deviation in region pulse - <strong>bin0_bg_mean</strong>: bin0 background mean in region of pulse - <strong>bin0_bg_std</strong>: bin0 background standard deviation in region pulse <strong>{run_id}.csv.gz</strong>: Compressed comma-separated value file containing RS/ROI properties computed from raw pulses.bin file by included RS caller (example in <strong>rs_caller.py</strong>). - <strong>ap</strong>: unique aperture index on chip - <strong>ROI</strong>: ordinal ROI number in the aperture, 0-indexed - <strong>start_p</strong>: index (.loc) of first pulse in the ROI (inclusive) in pulse dataframe - <strong>end_p</strong>: index (.loc) of last pulse in the ROI (inclusive) in pulse dataframe - <strong>start_f</strong>: first frame of the first pulse in the ROI (inclusive) - <strong>end_f</strong>: Last frame of the last pulse in the ROI (exclusive) - <strong>start_s</strong>: Time (in seconds elapsed from beginning of run) of the start of the ROI - <strong>end_s</strong>: Time (in seconds elapsed from beginning of run) of the end of the ROI - <strong>dur_f</strong>: Duration in frames of the ROI - <strong>dur_s</strong>: Duration in seconds of the ROI - <strong>num_pulses</strong>: Number of pulses in the ROI (that also passed filtering during ROI-calling) - <strong>pw_mean</strong>: Mean pulse duration (in seconds) of pulses in the ROI - <strong>ipd_mean</strong>: Mean inter-pulse duration (in seconds) of pulses in the ROI - <strong>snr_mean</strong>: Mean signal-to-noise ratio of pulses in the ROI - <strong>intensity_mean</strong>: Mean intensity above baseline of pulses in the ROI - <strong>binratio_norm</strong>: Estimated pulse bin ratio of pulses in the ROI, according to the following equation: sum(bin0_intensity*dur_f) / np.sum(bin1_intensity*dur_f) - <strong>ROI_score</strong>: ROI quality score (0-1 from least to most likely to contain recognizer-peptide recognition pulsing) - <strong>binratio_skew</strong>: bin ratio correction factor accounting for binning signal timing differences across the chip. This factor has already been applied to the binratio_norm column</pre>
Reinforcing Tunnel Network Exploration in Proteins using Gaussian Accelerated Molecular Dynamics (parameters, trajectories)
<ul> <li>00_LinB-Wt.tar.gz - LinB-Wt simulation files:</li> </ul> <p> 1.cMD(Classical MD simulation):<br> <br> 1. Stripped parameter file *.parm7.<br> 2. Simulation file after removing ions and water and merging last 5us of production run in amber *.nc format.<br> <br> <br> 2.GaMD(Gaussian Accelerated MD simulation): <br> <br> 1. Stripped parameter file *.parm7.<br> 2. Simulation file after removing ions and water and merging last 5us of production run in amber *.nc format.</p> <ul> <li>01_LinB-Open.tar.gz - LinB Open mutant simulation files:</li> </ul> <p> 1.cMD(Classical MD simulation):<br> <br> 1. Stripped parameter file *.parm7. <br> 2. Simulation file after removing ions and water and merging last 5us of production run in amber *.nc format.<br> <br> <br> 2.GaMD(Gaussian Accelerated MD simulation): <br> 1. Stripped parameter file *.parm7.<br> 2. Simulation file after removing ions and water and merging last 5us of production run in amber *.nc format.</p> <ul> <li>02_LinB-Closed.tar.gz - LinB Closed mutant simulation files:</li> </ul> <p> 1.cMD(Classical MD simulation):<br> 1. Stripped parameter file *.parm7.<br> 2. Simulation file after removing ions and water and merging last 5us of production run in amber *.nc format.<br> <br> <br> 2.GaMD(Gaussian Accelerated MD simulation): <br> 1. Stripped parameter file *.parm7.<br> 2. Simulation file after removing ions and water and merging last 5us of production run in amber *.nc format.</p>
Seasonal footprints on ecological time series and jumps in dynamic states of protein configurations from a nonlinear forecasting method characterization (DataSet)
<p>Data from the article: <br>"Seasonal footprints on ecological time series and jumps in dynamic states of protein configurations from a nonlinear forecasting method characterization", L. Reyes, K. Campos, G. D. Avendaño, L. González-Paz, A. Vivas, Y. J. Alvarado, and S. Flores.</p> <p>Data to be used with some implementation of the forecasting method of reference:<br>Sugihara G. and May R. M., Nonlinear forecasting as a way of distinguishing chaos from measurement error in time series, <em>Nature</em> <strong>344</strong>, 734–741 (1990).</p>
Nanoscale dipole dynamics of protein membranes studied by broadband dielectric microscopy
<p>Original data in support of our publication: Nanoscale dipole dynamics of protein membranes studied by broadband dielectric microscopy</p>
Supplementary Data for "Molecular dynamics simulations provide structural insight into binding of cyclic dinucleotides to human STING protein"
<p>Supplementary Data for "Molecular dynamics simulations provide structural insight into binding of cyclic dinucleotides to human STING protein", Journal of Biomolecular Structure and Dynamics, 2021, 10.1080/07391102.2021.1942213</p> <p>A random selection of 10 representative structures from each MSM state of STING/CDN complexes is provided in .pdb file format. The selected MSM representatives are aligned and available as PyMOL session files.</p>
Dataset (VII) related to publication: Decisive Role of Water and Protein Dynamics in Residence Time of p38a MAP Kinase Inhibitors
<p>MD simulation data of compound <strong>1</strong> in MSM <strong>2-<em>S</em><sub>3</sub></strong> conformations of the related to the publication Pantsar et al.: <em>Decisive Role of Water and Protein Dynamics in Residence Time of p38a MAP Kinase Inhibitors.</em></p> <p>Individual .zip files contain raw-desmond trajectories (-out.cms files and trj-files).</p> <p>All datasets related to this publication:</p> <p><a href="https://doi.org/10.5281/zenodo.4568113">https://doi.org/10.5281/zenodo.4568113</a>(compound <strong>1</strong>; dataset: I)</p> <p><a href="https://doi.org/10.5281/zenodo.4572444">https://doi.org/10.5281/zenodo.4572444</a> (compound <strong>1</strong>; dataset: II)</p> <p><a href="https://doi.org/10.5281/zenodo.4561797">https://doi.org/10.5281/zenodo.4561797</a>(compound <strong>2</strong>; dataset: III)</p> <p><a href="https://doi.org/10.5281/zenodo.4563896">https://doi.org/10.5281/zenodo.4563896</a> (compound <strong>2</strong>; dataset: IV)</p> <p><a href="https://doi.org/10.5281/zenodo.5563359">https://doi.org/10.5281/zenodo.5563359</a> (<strong>SB203580</strong>; dataset: V)</p> <p><a href="https://doi.org/10.5281/zenodo.5563655">https://doi.org/10.5281/zenodo.5563655</a> (<strong>SB203580</strong>; dataset: VI)</p> <p><a href="https://doi.org/10.5281/zenodo.5564118%20">https://doi.org/10.5281/zenodo.5564118 </a>(compound <strong>1</strong> simulated in compound <strong>2</strong> metastable state <strong>2-<em>S</em><sub>3</sub></strong>; dataset: VII)</p> <p><a href="https://doi.org/10.5281/zenodo.5564208%20">https://doi.org/10.5281/zenodo.5564208 </a>(compound <strong>1</strong> simulated in compound <strong>2</strong> metastable state <strong>2-<em>S</em><sub>3</sub></strong>; dataset: VIII)</p> <p><a href="https://doi.org/10.5281/zenodo.5564586">https://doi.org/10.5281/zenodo.5564586</a> (well-tempered metadynamics simulations of compounds <strong>1</strong> and <strong>2</strong>; dataset: IX)</p> <p><a href="https://doi.org/10.5281/zenodo.5570882">https://doi.org/10.5281/zenodo.5570882</a> (well-tempered metadynamics simulations of compounds <strong>1</strong> and <strong>2</strong>; dataset: X)</p> <p><a href="https://doi.org/10.5281/zenodo.5571352">https://doi.org/10.5281/zenodo.5571352</a> (well-tempered metadynamics simulations of compounds <strong>1</strong> and <strong>2</strong>; dataset: XI)</p> <p>The datasets include original Desmond raw-trajectories (datasets I–VIII), PDB-coordinates for the energy minimized metastable state derived structures (datasets II, IV and VI) and raw-trajectories of the well-tempered metadynamics simulations (dataset IX–XI).</p>
Dataset (VIII) related to publication: Decisive Role of Water and Protein Dynamics in Residence Time of p38a MAP Kinase Inhibitors
<p>MD simulation data of compound <strong>1</strong> in MSM <strong>2-<em>S</em><sub>3</sub></strong> conformations of the related to the publication Pantsar et al.: <em>Decisive Role of Water and Protein Dynamics in Residence Time of p38a MAP Kinase Inhibitors.</em></p> <p>Individual .zip files contain raw-desmond trajectories (-out.cms files and trj-files).</p> <p>All datasets related to this publication:</p> <p><a href="https://doi.org/10.5281/zenodo.4568113">https://doi.org/10.5281/zenodo.4568113</a>(compound <strong>1</strong>; dataset: I)</p> <p><a href="https://doi.org/10.5281/zenodo.4572444">https://doi.org/10.5281/zenodo.4572444</a> (compound <strong>1</strong>; dataset: II)</p> <p><a href="https://doi.org/10.5281/zenodo.4561797">https://doi.org/10.5281/zenodo.4561797</a>(compound <strong>2</strong>; dataset: III)</p> <p><a href="https://doi.org/10.5281/zenodo.4563896">https://doi.org/10.5281/zenodo.4563896</a> (compound <strong>2</strong>; dataset: IV)</p> <p><a href="https://doi.org/10.5281/zenodo.5563359">https://doi.org/10.5281/zenodo.5563359</a> (<strong>SB203580</strong>; dataset: V)</p> <p><a href="https://doi.org/10.5281/zenodo.5563655">https://doi.org/10.5281/zenodo.5563655</a> (<strong>SB203580</strong>; dataset: VI)</p> <p><a href="https://doi.org/10.5281/zenodo.5564118%20">https://doi.org/10.5281/zenodo.5564118 </a>(compound <strong>1</strong> simulated in compound <strong>2</strong> metastable state <strong>2-<em>S</em><sub>3</sub></strong>; dataset: VII)</p> <p><a href="https://doi.org/10.5281/zenodo.5564208%20">https://doi.org/10.5281/zenodo.5564208 </a>(compound <strong>1</strong> simulated in compound <strong>2</strong> metastable state <strong>2-<em>S</em><sub>3</sub></strong>; dataset: VIII)</p> <p><a href="https://doi.org/10.5281/zenodo.5564586">https://doi.org/10.5281/zenodo.5564586</a> (well-tempered metadynamics simulations of compounds <strong>1</strong> and <strong>2</strong>; dataset: IX)</p> <p><a href="https://doi.org/10.5281/zenodo.5570882">https://doi.org/10.5281/zenodo.5570882</a> (well-tempered metadynamics simulations of compounds <strong>1</strong> and <strong>2</strong>; dataset: X)</p> <p><a href="https://doi.org/10.5281/zenodo.5571352">https://doi.org/10.5281/zenodo.5571352</a> (well-tempered metadynamics simulations of compounds <strong>1</strong> and <strong>2</strong>; dataset: XI)</p> <p>The datasets include original Desmond raw-trajectories (datasets I–VIII), PDB-coordinates for the energy minimized metastable state derived structures (datasets II, IV and VI) and raw-trajectories of the well-tempered metadynamics simulations (dataset IX–XI).</p>
Dataset (V) related to publication: Decisive Role of Water and Protein Dynamics in Residence Time of p38a MAP Kinase Inhibitors
<p>MD simulation data of <strong>SB203580</strong> related to the publication Pantsar et al.: <em>Decisive Role of Water and Protein Dynamics in Residence Time of p38a MAP Kinase Inhibitors.</em></p> <p>Individual .zip files contain raw-desmond trajectories (-out.cms files and trj-files).</p> <p>All datasets related to this publication:</p> <p><a href="https://doi.org/10.5281/zenodo.4568113">https://doi.org/10.5281/zenodo.4568113</a>(compound <strong>1</strong>; dataset: I)</p> <p><a href="https://doi.org/10.5281/zenodo.4572444">https://doi.org/10.5281/zenodo.4572444</a> (compound <strong>1</strong>; dataset: II)</p> <p><a href="https://doi.org/10.5281/zenodo.4561797">https://doi.org/10.5281/zenodo.4561797</a>(compound <strong>2</strong>; dataset: III)</p> <p><a href="https://doi.org/10.5281/zenodo.4563896">https://doi.org/10.5281/zenodo.4563896</a> (compound <strong>2</strong>; dataset: IV)</p> <p><a href="https://doi.org/10.5281/zenodo.5563359">https://doi.org/10.5281/zenodo.5563359</a> (<strong>SB203580</strong>; dataset: V)</p> <p><a href="https://doi.org/10.5281/zenodo.5563655">https://doi.org/10.5281/zenodo.5563655</a> (<strong>SB203580</strong>; dataset: VI)</p> <p><a href="https://doi.org/10.5281/zenodo.5564118%20">https://doi.org/10.5281/zenodo.5564118 </a>(compound <strong>1</strong> simulated in compound <strong>2</strong> metastable state <strong>2-<em>S</em><sub>3</sub></strong>; dataset: VII)</p> <p><a href="https://doi.org/10.5281/zenodo.5564208%20">https://doi.org/10.5281/zenodo.5564208 </a>(compound <strong>1</strong> simulated in compound <strong>2</strong> metastable state <strong>2-<em>S</em><sub>3</sub></strong>; dataset: VIII)</p> <p><a href="https://doi.org/10.5281/zenodo.5564586">https://doi.org/10.5281/zenodo.5564586</a> (well-tempered metadynamics simulations of compounds <strong>1</strong> and <strong>2</strong>; dataset: IX)</p> <p><a href="https://doi.org/10.5281/zenodo.5570882">https://doi.org/10.5281/zenodo.5570882</a> (well-tempered metadynamics simulations of compounds <strong>1</strong> and <strong>2</strong>; dataset: X)</p> <p><a href="https://doi.org/10.5281/zenodo.5571352">https://doi.org/10.5281/zenodo.5571352</a> (well-tempered metadynamics simulations of compounds <strong>1</strong> and <strong>2</strong>; dataset: XI)</p> <p>The datasets include original Desmond raw-trajectories (datasets I–VIII), PDB-coordinates for the energy minimized metastable state derived structures (datasets II, IV and VI) and raw-trajectories of the well-tempered metadynamics simulations (dataset IX–XI).</p>
Data deposition for "Reliability and accuracy of single-molecule FRET studies for characterization of structural dynamics and distances in proteins"
<p>The deposited data for the publication "Reliability and accuracy of single-molecule FRET studies for characterization of structural dynamics and distances in proteins".</p> <p>Data contains folder and sub-folders for the raw data, Main excel sheet named as "MasterTable_FRET-Challenge-Protein-Dynamics_Nat_Meth_Agam et al" has most of the data used in the publication. Another excel sheets "Data List for FIgures for Agam et al_revised" and "Data List for Supplmentary FIgures for Agam et al_revised" have the information regarding the Figure-wise data description and where the respective data locates.</p>
Data for manuscript "Adaptive Ensemble Refinement of Protein Structures in High Resolution Electron Microscopy Density Maps with Radical Augmented Molecular Dynamics Flexible Fitting"
<p>The tar file contains the input files for RADICAL augmented MDFF implementation (R-MDFF) for two protein systems, Adenylate Kinase (ADK) and Carbon Monoxide Dehydrogenase (CODH). These examples demonstrate the implementation of R-MDFF using RADICAL-Cybertools to flexibly fit biomolecules in cryo-EM density maps with on-the-fly decision making.</p> <p>All molecular simulations were performed using CUDA enabled NAMD 2.14 installed on OLCF Summit HPC resource. The CHARMM36 force field parameters were used for the proteins. Synthetic density maps were prepared at 1.8, 3 and 5 Å for ADK and 1.8 and 3 Å for CODH using VMD 1.9.3 software installed on OLCF Summit HPC resource. During the analysis stage, the cross correlation coefficients between density maps and atomic model were computed using VMD 1.9.3 on Summit HPC as part of the R-MDFF workflow.</p> <p>The source code is publicly available on GitHub: <a href="https://github.com/radical-collaboration/MDFF-EnTK">https://github.com/radical-collaboration/MDFF-EnTK </a></p> <p>The preprint of this research is submitted on bioRxiv, doi: <a href="https://doi.org/10.1101/2021.12.07.471672">https://doi.org/10.1101/2021.12.07.471672 </a></p> <p>To obtain maximum compression of the data, the tar command used to generate this tarball was:</p> <pre><code class="language-bash">GZIP=-9 tar --exclude='last.pdb' --exclude='*last_from_prev_iter.pdb' --exclude='*old' --exclude='*log' --exclude='*coor' --exclude='*vel' --exclude='*xsc' --exclude='*dcd' --exclude='lastframepdbs_fix' --exclude='*out' --exclude='*sl' --exclude='*rs' --exclude='*prof' --exclude='*err' --exclude='*dx' --exclude='*grid.pdb' --exclude='*txt' -cvzf rmdffv2.tar.gz rmdff-zenodo/</code></pre> <p> </p>
ScienceDex guides
Understand access before you commit
These curated guides explain access requirements, typical timelines, costs, and reuse considerations for widely used research datasets.
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.