<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Tranchant EE</submitter><funding>Københavns Universitet</funding><funding>Danmarks Frie Forskningsfond</funding><funding>Novo Nordisk Fonden</funding><funding>Lundbeck Foundation</funding><pagination>3759-3770</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11560309</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>123(21)</volume><pubmed_abstract>Measuring the compaction of a protein or complex is key to our understanding of the interactions within and between biomolecules. Experimentally, protein compaction is often probed either by estimating the radius of gyration (R&lt;sub>g&lt;/sub>) obtained from small-angle x-ray scattering (SAXS) experiments or the hydrodynamic radius (R&lt;sub>h&lt;/sub>) obtained, for example, by pulsed field gradient NMR (PFG NMR) spectroscopy. PFG NMR experiments generally report on the translational diffusion coefficient, which in turn can be used to estimate R&lt;sub>h&lt;/sub> using an internal standard to account for sample viscosity and uncertainty about the gradient strength. 1,4-Dioxane is one such commonly used internal standard, and the reference value of R&lt;sub>h&lt;/sub> is therefore important. We have revisited t</pubmed_abstract><journal>Biophysical journal</journal><pubmed_title>On the use of dioxane as reference for determination of the hydrodynamic radius by NMR spectroscopy.</pubmed_title><pmcid>PMC11560309</pmcid><funding_grant_id>R155-2015-2666</funding_grant_id><funding_grant_id>9040-00164B</funding_grant_id><funding_grant_id>NNF18OC0033950</funding_grant_id><funding_grant_id>NNF18OC0033926</funding_grant_id><funding_grant_id>NNF19OC0055857</funding_grant_id><pubmed_authors>Lindorff-Larsen K</pubmed_authors><pubmed_authors>Kragelund BB</pubmed_authors><pubmed_authors>Fernandes CB</pubmed_authors><pubmed_authors>Pesce F</pubmed_authors><pubmed_authors>Tranchant EE</pubmed_authors><pubmed_authors>Jacobsen NL</pubmed_authors></additional><is_claimable>false</is_claimable><name>On the use of dioxane as reference for determination of the hydrodynamic radius by NMR spectroscopy.</name><description>Measuring the compaction of a protein or complex is key to our understanding of the interactions within and between biomolecules. Experimentally, protein compaction is often probed either by estimating the radius of gyration (R&lt;sub>g&lt;/sub>) obtained from small-angle x-ray scattering (SAXS) experiments or the hydrodynamic radius (R&lt;sub>h&lt;/sub>) obtained, for example, by pulsed field gradient NMR (PFG NMR) spectroscopy. PFG NMR experiments generally report on the translational diffusion coefficient, which in turn can be used to estimate R&lt;sub>h&lt;/sub> using an internal standard to account for sample viscosity and uncertainty about the gradient strength. 1,4-Dioxane is one such commonly used internal standard, and the reference value of R&lt;sub>h&lt;/sub> is therefore important. We have revisited t</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Nov</publication><modification>2026-06-05T11:49:32.838Z</modification><creation>2026-05-16T03:13:31.663Z</creation></dates><accession>S-EPMC11560309</accession><cross_references><pubmed>39340154</pubmed><doi>10.1016/j.bpj.2024.09.025</doi></cross_references></HashMap>