{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Marincin KA"],"funding":["Flight Attendant Medical Research Institute","NCATS NIH HHS","Institute for Clinical and Translational Research, University of Maryland, Baltimore","National Institutes of Health","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["107265"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9463103"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["342"],"pubmed_abstract":["The non-invasive nature of NMR offers a means to monitor biochemical reactions in situ at the atomic level. We harness this advantage to monitor a complex chemoenzymatic reaction that sequentially modifies reagents and loads the product on a nonribosomal peptide synthetase carrier protein. We present a protocol including a pulse sequence that permits to assess both the integrity of reagents and the completion of each step in the reaction, thus alleviating otherwise time-consuming and costly approaches to debug and repeat inefficient reactions. This study highlights the importance of NMR as a tool to establish reliable and reproducible experimental conditions in biochemical studies."],"journal":["Journal of magnetic resonance (San Diego, Calif. : 1997)"],"pubmed_title":["NMR as a readout to monitor and restore the integrity of complex chemoenzymatic reactions."],"pmcid":["PMC9463103"],"funding_grant_id":["R01 GM104257","UL1 TR003098","R01GM104257","UL1TR003098","T32 GM080189"],"pubmed_authors":["Meyers DJ","Kengmana ES","Marincin KA","Frueh DP","Hwang Y"],"additional_accession":[]},"is_claimable":false,"name":"NMR as a readout to monitor and restore the integrity of complex chemoenzymatic reactions.","description":"The non-invasive nature of NMR offers a means to monitor biochemical reactions in situ at the atomic level. We harness this advantage to monitor a complex chemoenzymatic reaction that sequentially modifies reagents and loads the product on a nonribosomal peptide synthetase carrier protein. We present a protocol including a pulse sequence that permits to assess both the integrity of reagents and the completion of each step in the reaction, thus alleviating otherwise time-consuming and costly approaches to debug and repeat inefficient reactions. This study highlights the importance of NMR as a tool to establish reliable and reproducible experimental conditions in biochemical studies.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-05-28T01:36:13.567Z","creation":"2024-11-09T11:20:10.345Z"},"accession":"S-EPMC9463103","cross_references":{"pubmed":["35849973"],"doi":["10.1016/j.jmr.2022.107265"]}}