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We present two complementary\n                    <jats:sup>13<\/jats:sup>\n                    C\u2010detected NMR strategies that exploit multiple acquisition schemes to simultaneously monitor positively and negatively charged residues. A \u201cNMR by Ordered Acquisition using\n                    <jats:sup>1<\/jats:sup>\n                    H detection (NOAH)\u201d\u2010based experiment combines C\n                    <jats:sub>\u03b6<\/jats:sub>\n                    N\n                    <jats:sub>\u03b7<\/jats:sub>\n                    \u2010HDQC and SC\u2010CACO experiments, allowing the simultaneous detection of arginine, aspartate, and glutamate side chains resonances. In parallel, the Multiple\u2010Receiver (MR) strategy integrates CP\u2010HISQC and C\n                    <jats:sub>\u03b6<\/jats:sub>\n                    N\n                    <jats:sub>\u03b5<\/jats:sub>\n                    \u2010HSQC, allowing full assignment of the arginine guanidinium group. We apply this approach to study the interaction between the SARS\u2010CoV\u20102 nucleocapsid N\u2010terminal domain and the negatively charged glycosaminoglycan enoxaparin. The experiments provide information about flexible, charged side chains at the protein ligand interface. Together, NOAH and MR approaches provide a powerful framework for the high\u2010resolution characterization of charged side chains and electrostatically driven interactions.\n                  <\/jats:p>","DOI":"10.1002\/pro.70533","type":"journal-article","created":{"date-parts":[[2026,3,13]],"date-time":"2026-03-13T14:12:54Z","timestamp":1773411174000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["At the core of the interaction: Probing charged side chains in flexible protein regions with simultaneous nuclear magnetic resonance experiments"],"prefix":"10.1002","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0053-0864","authenticated-orcid":false,"given":"Maria Anna","family":"Rodella","sequence":"first","affiliation":[{"name":"Department of Chemistry \u201cUgo Schiff\u201d and Magnetic Resonance Center (CERM) University of Florence  Florence 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