{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Haller JD"],"funding":["Helmholtz-Gemeinschaft","Deutsche Forschungsgemeinschaft","Nemzeti Kutatási Fejlesztési és Innovációs Hivatal","Karlsruher Institut für Technologie (KIT)"],"pagination":["213-221"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9712348"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["76(5-6)"],"pubmed_abstract":["Large coupling networks in uniformly <sup>13</sup>C,<sup>15</sup>N-labeled biomolecules induce broad multiplets that even in flexible proteins are frequently not recognized as such. The reason is that given multiplets typically consist of a large number of individual resonances that result in a single broad line, in which individual components are no longer resolved. We here introduce a real-time pure shift acquisition scheme for the detection of amide protons which is based on <sup>13</sup>C-BIRD<sup>r,X</sup>. As a result the full homo- and heteronuclear coupling network can be suppressed at low power leading to real singlets at substantially improved resolution and uncompromised sensitivity. The method is tested on a small globular and an intrinsically disordered protein (IDP) where the average spectral resolution is increased by a factor of ~ 2 and higher. Equally important, the approach works without saturation of water magnetization for solvent suppression and exchanging amide protons are not affected by saturation transfer."],"journal":["Journal of biomolecular NMR"],"pubmed_title":["Pure shift amide detection in conventional and TROSY-type experiments of <sup>13</sup>C,<sup>15</sup>N-labeled proteins."],"pmcid":["PMC9712348"],"funding_grant_id":["LU 835/13-1","K137940","Information 43.35.02","K124900"],"pubmed_authors":["Bodor A","Haller JD","Luy B"],"additional_accession":[]},"is_claimable":false,"name":"Pure shift amide detection in conventional and TROSY-type experiments of <sup>13</sup>C,<sup>15</sup>N-labeled proteins.","description":"Large coupling networks in uniformly <sup>13</sup>C,<sup>15</sup>N-labeled biomolecules induce broad multiplets that even in flexible proteins are frequently not recognized as such. The reason is that given multiplets typically consist of a large number of individual resonances that result in a single broad line, in which individual components are no longer resolved. We here introduce a real-time pure shift acquisition scheme for the detection of amide protons which is based on <sup>13</sup>C-BIRD<sup>r,X</sup>. As a result the full homo- and heteronuclear coupling network can be suppressed at low power leading to real singlets at substantially improved resolution and uncompromised sensitivity. The method is tested on a small globular and an intrinsically disordered protein (IDP) where the average spectral resolution is increased by a factor of ~ 2 and higher. Equally important, the approach works without saturation of water magnetization for solvent suppression and exchanging amide protons are not affected by saturation transfer.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-18T16:54:46.868Z","creation":"2025-04-07T04:21:38.175Z"},"accession":"S-EPMC9712348","cross_references":{"pubmed":["36399207"],"doi":["10.1007/s10858-022-00406-z"]}}