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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
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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