<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Christensen S</submitter><funding>Swedish Research Council for Environment Agricultural Sciences and Spatial Planning</funding><funding>Mats Paulsson Foundation</funding><funding>Swedish Research Council</funding><pagination>3973</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9961634</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>24(4)</volume><pubmed_abstract>Plant hemoglobins, often referred to as phytoglobins, play important roles in abiotic stress tolerance. Several essential small physiological metabolites can be bound to these heme proteins. In addition, phytoglobins can catalyze a range of different oxidative reactions in vivo. These proteins are often oligomeric, but the degree and relevance of subunit interactions are largely unknown. In this study, we delineate which residues are involved in dimer formation of a sugar beet phytoglobin type 1.2 (BvPgb1.2) using NMR relaxation experiments. &lt;i>E. coli&lt;/i> cells harboring a phytoglobin expression vector were cultivated in isotope-labeled (&lt;sup>2&lt;/sup>H, &lt;sup>13&lt;/sup>C and &lt;sup>15&lt;/sup>N) M9 medium. The triple-labeled protein was purified to homogeneity using two chromatographic steps. Two </pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>Conformational Dynamics of Phytoglobin BvPgb1.2 from &lt;i>Beta vulgaris&lt;/i> ssp. &lt;i>vulgaris&lt;/i>.</pubmed_title><pmcid>PMC9961634</pmcid><funding_grant_id>2019</funding_grant_id><funding_grant_id>2020-0185</funding_grant_id><funding_grant_id>2019-03996</funding_grant_id><funding_grant_id>2020-01855</funding_grant_id><pubmed_authors>Akke M</pubmed_authors><pubmed_authors>Stenstrom O</pubmed_authors><pubmed_authors>Bulow L</pubmed_authors><pubmed_authors>Christensen S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Conformational Dynamics of Phytoglobin BvPgb1.2 from &lt;i>Beta vulgaris&lt;/i> ssp. &lt;i>vulgaris&lt;/i>.</name><description>Plant hemoglobins, often referred to as phytoglobins, play important roles in abiotic stress tolerance. Several essential small physiological metabolites can be bound to these heme proteins. In addition, phytoglobins can catalyze a range of different oxidative reactions in vivo. These proteins are often oligomeric, but the degree and relevance of subunit interactions are largely unknown. In this study, we delineate which residues are involved in dimer formation of a sugar beet phytoglobin type 1.2 (BvPgb1.2) using NMR relaxation experiments. &lt;i>E. coli&lt;/i> cells harboring a phytoglobin expression vector were cultivated in isotope-labeled (&lt;sup>2&lt;/sup>H, &lt;sup>13&lt;/sup>C and &lt;sup>15&lt;/sup>N) M9 medium. The triple-labeled protein was purified to homogeneity using two chromatographic steps. Two </description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Feb</publication><modification>2025-04-05T07:24:31.748Z</modification><creation>2025-04-05T07:24:31.748Z</creation></dates><accession>S-EPMC9961634</accession><cross_references><pubmed>36835381</pubmed><doi>10.3390/ijms24043973</doi></cross_references></HashMap>