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4 results for “Protein solvation”

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zenodo44/100

DATASET: Protein Binding Leads to Reduced Stability and Solvated Disorder in the Polystyrene Nanoparticle Corona

<p>This dataset contains the DLS, CD, fluorescence, ITC, TEM, and ANS raw data used for the manuscript.</p>

opencc-by-4.0Jul 2023View details →
zenodo40/100

Solvated protein fragments

<p>The solvated protein fragments dataset probes many-body intermolecular interactions between&nbsp;<br> &quot;protein fragments&quot; and water molecules, which are important for the description of many&nbsp;<br> biologically relevant condensed phase systems. It contains structures for all possible&nbsp;<br> &quot;amons&quot; [1] (hydrogen-saturated covalently bonded fragments) of up to eight heavy atoms&nbsp;<br> (C, N, O, S) that can be derived from chemical graphs of proteins containing the 20 natural<br> amino acids connected via peptide bonds or disulfide bridges. For amino acids that can occur&nbsp;<br> in different charge states due to (de-)protonation (i.e. carboxylic acids that can be&nbsp;<br> negatively charged or amines that can be positively charged), all possible structures with&nbsp;<br> up to a total charge of +-2e are included. In total, the dataset provides reference energies,&nbsp;<br> forces, and dipole moments for 2731180 structures calculated at the revPBE-D3(BJ)/def2-TZVP&nbsp;<br> level of theory [2-5] using the ORCA 4.0.1 code [6,7].&nbsp;</p> <p>For more details, see https://arxiv.org/abs/1902.08408.</p> <p>[1] Huang, B. and von Lilienfeld, O. A. arXiv:1707.04146 (2017).<br> [2] Grimme, S.; Antony, J.; Ehrlich, S. and Krieg, H. J. Chem. Phys. 132, 154104 (2010).<br> [3] Grimme, S.; Ehrlich, S. and Goerigk, L. J. Comput. Chem. 32, 1456-1465 (2011).<br> [4] Weigend, F. and Ahlrichs, R. Phys. Chem. Chem. Phys. 7, 3297-3305 (2005).<br> [5] Zhang, Y. and Yang, W. Phys. Rev. Lett. 80, 890 (1998).<br> [6] Neese, F. Wiley Interdiscip. Rev. Comput. Mol. Sci. 2, 73-78 (2012).<br> [7] Neese, F. Wiley Interdiscip. Rev. Comput. Mol. Sci. 8, e1327 (2018).</p>

opencc-by-4.0Mar 2019View details →
zenodo36/100

Solvated Protein Fragments (QCArchive View Formatted)

<p>Data curated by the QCArchive team, originally sourced from quantum-machine.org.</p> <p>Water-solvated protein fragments with up to 8 heavy atoms. Configurations are generated from MD, evaluated at the revPBE-D3(BJ)/def2-TZVP level of theory. Also included are fragment dimers and clusters of up to 40 water molecules.</p> <p>For more information, see http://qcarchive.molssi.org/apps/ml_datasets/.</p>

opencc-by-4.0Nov 2019View details →
zenodo32/100

DOX_BDW: Incorporating Solvation and Desolvation Effects of Cavity Water into Nonfitting Protein–Ligand Binding Affinity Prediction

<p><strong>structures.zip:</strong>&nbsp;&nbsp;including&nbsp;the&nbsp;coordinates&nbsp;of&nbsp;all&nbsp;optimized&nbsp;proteinligand&nbsp;complex&nbsp;structure&nbsp;obtained&nbsp;by&nbsp;DOX_BDW&nbsp;calculation.&nbsp;(compressed&nbsp;PDB&nbsp;file).&nbsp;These&nbsp;pdb&nbsp;files&nbsp;could&nbsp;also&nbsp;be&nbsp;&nbsp;used&nbsp;as&nbsp;input&nbsp;for&nbsp;the&nbsp;binding&nbsp;energy&nbsp;calculation,as&nbsp;illustrated&nbsp;in&nbsp;SI&nbsp;section&nbsp;8.&nbsp;</p> <p><strong>mdinput.zip:</strong>&nbsp;Including&nbsp;the&nbsp;input&nbsp;files,parameter&nbsp;files,&nbsp;topology&nbsp;files&nbsp;needed&nbsp;to&nbsp;run&nbsp;MD&nbsp;simulation&nbsp;for&nbsp;water&nbsp;mapping,&nbsp;as&nbsp;illustrated&nbsp;in&nbsp;SI&nbsp;section&nbsp;8.&nbsp;Note&nbsp;that&nbsp;all&nbsp;of&nbsp;the&nbsp;parameter&nbsp;files&nbsp;and&nbsp;topology&nbsp;files&nbsp;would&nbsp;be&nbsp;automatically&nbsp;generated&nbsp;using&nbsp;the&nbsp;RUNMD&nbsp;program&nbsp;we&nbsp;uploaded&nbsp;with&nbsp;the&nbsp;example&nbsp;file.&nbsp;</p> <p><strong>example.zip:</strong>&nbsp;The&nbsp;programs&nbsp;and&nbsp;input&nbsp;files&nbsp;needed&nbsp;to&nbsp;run&nbsp;an&nbsp;example,&nbsp;as&nbsp;illustrated&nbsp;in&nbsp;SI&nbsp;section&nbsp;9. And all the output files except&nbsp;MD&nbsp;trajectories&nbsp;are in there,too.</p>

opencc-by-4.0Jun 2023View details →

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International Brain Laboratory public data

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Last verified 2026-04-29Open record

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neuroscienceopenPublished datasets are available on demand over the internet.
Last verified 2026-04-29Open record