Enlarging the scenario of site directed 19F labeling for NMR spectroscopy of biomolecules

被引：5

作者：

Vitali, Valentina ^{[1
,2
]}

Torricella, Francesco ^{[1
]}

Massai, Lara ^{[2
]}

Messori, Luigi ^{[2
]}

Banci, Lucia ^{[1
,2
,3
]}

机构：

[1] Univ Florence, Magnet Resonance Ctr CERM, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy

[2] Univ Florence, Dept Chem Ugo Schiff, Via Lastruccia 3, I-50019 Sesto Fiorentino, Italy

[3] Consorzio Interuniv Risonanze Magnet Metalloprotei, Florence, Italy

来源：

SCIENTIFIC REPORTS | 2023年 / 13卷 / 01期

基金：

欧盟地平线“2020”;

关键词：

PROTEIN-STRUCTURE; TYROSINE BIOCONJUGATION; SURFACE MODIFICATION; EPR SPECTROSCOPY; NITRIC-OXIDE; PROBE; BINDING; DOMAIN; OXYGEN; GB1;

D O I：

10.1038/s41598-023-49247-2

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The possibility of using selectively incorporated F-19 nuclei for NMR spectroscopic studies has retrieved increasing interest in recent years. The high gyromagnetic ratio of F-19 and its absence in native biomolecular systems make this nucleus an interesting alternative to standard H-1 NMR spectroscopy. Here we show how we can attach a label, carrying a F-19 atom, to protein tyrosines, through the use of a specific three component Mannich-type reaction. To validate the efficacy and the specificity of the approach, we tested it on two selected systems with the aid of ESI MS measurements.

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页数：9

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