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5 results for “coacervate”

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zenodo48/100

Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau

<p><strong><em>The following metadata refers exclusively to electron paramagnetic resonance (EPR) measurements, which represent the contribution of the PARACAT students to this work</em></strong></p> <ul> <li><strong>Data type</strong>: EPR spectroscopic measurements and simulations</li> <li>Files are in <strong>.DTA, .DSC, .m, .mat, and .xlxs, </strong>formats</li> <li>Information on <strong>origin of the data</strong>: <ul> <li>EPR spectroscopic measurements in <strong>.DTA </strong>and<strong> .DSC</strong> formats</li> <li>EPR spectroscopic simulation and analyses in .<strong>m </strong>and<strong> .mat</strong> format</li> <li>&ldquo;Ready-to-plot&rdquo;, processed EPR spectra are in <strong>.xlxs</strong> format.</li> </ul> </li> <li>The data are <strong>generated</strong> by: <ul> <li>CW-EPR measurements were performed with a Bruker ELEXSYS E580 X-band spectrometer equipped with a Bruker ER4118 SPT-N1 resonator operating at a microwave (MW) frequency of &sim;9.7 GHz. The temperature was set to 25 &deg;C and controlled by a liquid nitrogen cryostat.</li> </ul> </li> </ul> <p>&nbsp;</p> <ul> <li><strong>If the dataset includes multiple files that relate to each other:</strong> <ul> <li>Files in <strong>PARACAT_WP3_20221219_EPR </strong>folder includes EPR spectroscopic measurements and computer simulations/analyses, original data are in <strong>&nbsp;.DTA/.DSC</strong> formats; files in .<strong>m</strong> format were used to process the data.</li> </ul> </li> </ul> <p>NB. See the &ldquo;READ ME&rdquo; text file for more detailed information on files organization.</p> <p>&nbsp;</p> <ul> <li><strong>Information on</strong>: <ul> <li>Abbreviations: <ul> <li><strong>avg</strong> = averaged</li> <li><strong>aS_24</strong> = alpha-synuclein protein with TEMPOL spin label at position 24 of the polypeptidic chain</li> <li><strong>aS_122</strong> = alpha-synuclein protein with TEMPOL spin label at position 122 of the polypeptidic chain</li> <li><strong>pLK</strong> = poly-lysine</li> <li><strong>Tau441</strong> = Tau protein with complete amino-acid sequence</li> <li><strong>Tau_DNt</strong> = truncated Tau protein lacking N-terminal (see paper methods for further details)</li> </ul> </li> <li>Units of measurement: <ul> <li>Temperature: <strong>&deg;</strong><strong>C</strong> (Celsius)</li> <li>Microwave Frequency: <strong>GHz</strong> (Giga-Hertz), <strong>MHz</strong> (Mega-Hertz), <strong>kHz</strong> (kilo-Hertz)</li> <li>Microwave Power: <strong>mW</strong> (milli-Watt)</li> <li>Magnetic Field: <strong>mT</strong> (milli-Tesla)</li> <li>Time: <strong>s</strong> (seconds)</li> <li>Concentration: <strong>&mu;M</strong> (micro-Molar), <strong>% w/v</strong> (percentage weight-volume)</li> </ul> </li> </ul> </li> </ul>

opencc-by-4.0Dec 2022View details →
dryad36/100

A coacervate-based mixed-conducting binder for high-power, high-energy batteries

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publicJun 2023View details →
dryad32/100

Data from: Flow imaging microscopy as a novel tool for high-throughput evaluation of elastin-like polymer coacervates

Biological and bioinspired polymer microparticles have broad biomedical and industrial applications, including drug delivery, tissue engineering, surface modification, environmental remediation, imaging, and sensing. Full realization of the potential of biopolymer microparticles will require methods for rigorous characterization of particle sizes, morphologies, and dynamics, so that researchers may correlate particle characteristics with synthesis methods and desired functions. Toward this end, we evaluated biopolymer microparticles using flow imaging microscopy. This technology is widely used in the biopharmaceutical industry but is not yet well-known among the materials community. Our polymer, a genetically engineered elastin-like polypeptide (ELP), self-assembles into micron-scale coacervates. We performed flow imaging of ELP coacervates using two different instruments, one with a lower size limit of approximately 2 microns, the other with a lower size limit of approximately 300 nanometers. We validated flow imaging results by comparison with dynamic light scattering and atomic force microscopy analyses. We explored the effects of various solvent conditions on ELP coacervate size, morphology, and behavior, such as the dispersion of single particles versus aggregates. We found that flow imaging is a superior tool for rapid and thorough particle analysis of ELP coacervates in solution. We anticipate that researchers studying many types of microscale protein or polymer assemblies will be interested in flow imaging as a tool for quantitative, solution-based characterization.

opencc-zeroJul 2019View details →
dryad32/100

Data from: Flow imaging microscopy as a novel tool for high-throughput evaluation of elastin-like polymer coacervates

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publicJul 2019View details →
zenodo28/100

Enzyme Immobilization with Plant-based Polysaccharides through Complex Coacervation

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opencc-by-4.0Nov 2024View details →

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