In-Cell NMR: Analysis of Protein-Small Molecule Interactions, Metabolic Processes, and Protein Phosphorylation

被引：11
作者：
Kumar, Amit [1 ,2 ,3 ]
Kuhn, Lars T. [1 ]
Balbach, Jochen [2 ,4 ]
机构：
[1] Univ Leeds, Sch Mol & Cellular Biol, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England
[2] Martin Luther Univ Halle Wittenberg, Inst Phys, Biophys, D-06120 Halle, Germany
[3] Kings Coll London, Fac Lifesci & Med, Dept Diabet, London SE1 1UL, England
[4] Martin Luther Univ Halle Wittenberg, Ctr Struct & Dynam Proteins MZP, D-06120 Halle, Germany
来源：
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2019年 / 20卷 / 02期
关键词：
protein NMR; in-cell NMR; in-situ NMR; DNP; review; PARATHYROID-HORMONE PTH; LIVING ESCHERICHIA-COLI; PROLYL ISOMERASE; PARA-HYDROGEN; POSTTRANSLATIONAL MODIFICATIONS; MULTIDIMENSIONAL NMR; F-19; NMR; SPECTROSCOPY; DOMAIN; HYPERPOLARIZATION;
D O I：
10.3390/ijms20020378
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Nuclear magnetic resonance (NMR) spectroscopy enables the non-invasive observation of biochemical processes, in living cells, at comparably high spectral and temporal resolution. Preferably, means of increasing the detection limit of this powerful analytical method need to be applied when observing cellular processes under physiological conditions, due to the low sensitivity inherent to the technique. In this review, a brief introduction to in-cell NMR, protein-small molecule interactions, posttranslational phosphorylation, and hyperpolarization NMR methods, used for the study of metabolites in cellulo, are presented. Recent examples of method development in all three fields are conceptually highlighted, and an outlook into future perspectives of this emerging area of NMR research is given.
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页数：23
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共 130 条
[1]   A theoretical basis for spontaneous polarization transfer in non-hydrogenative parahydrogen-induced polarization [J].
Adams, Ralph W. ;
Duckett, Simon B. ;
Green, Richard A. ;
Williamson, David C. ;
Green, Gary G. R. .
JOURNAL OF CHEMICAL PHYSICS, 2009, 131 (19)
[2]   Reversible Interactions with para-Hydrogen Enhance NMR Sensitivity by Polarization Transfer [J].
Adams, Ralph W. ;
Aguilar, Juan A. ;
Atkinson, Kevin D. ;
Cowley, Michael J. ;
Elliott, Paul I. P. ;
Duckett, Simon B. ;
Green, Gary G. R. ;
Khazal, Iman G. ;
Lopez-Serrano, Joaqun ;
Williamson, David C. .
SCIENCE, 2009, 323 (5922) :1708-1711
[3]   Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy [J].
Amata, Irene ;
Maffei, Mariano ;
Igea, Ana ;
Gay, Marina ;
Vilaseca, Marta ;
Nebreda, Angel R. ;
Pons, Miquel .
CHEMBIOCHEM, 2013, 14 (14) :1820-1827
[4]   Hyperpolarized Butyrate: A Metabolic Probe of Short Chain Fatty Acid Metabolism in the Heart [J].
Ball, Daniel R. ;
Rowlands, Ben ;
Dodd, Michael S. ;
Le Page, Lydia ;
Ball, Vicky ;
Carr, Carolyn A. ;
Clarke, Kieran ;
Tyler, Damian J. .
MAGNETIC RESONANCE IN MEDICINE, 2014, 71 (05) :1663-1669
[5]   Visualization of Redox-Controlled Protein Fold in Living Cells [J].
Banci, Lucia ;
Barbieri, Letizia ;
Luchinat, Enrico ;
Secci, Erica .
CHEMISTRY & BIOLOGY, 2013, 20 (06) :747-752
[6]  
Banci L, 2013, NAT CHEM BIOL, V9, P297, DOI [10.1038/NCHEMBIO.1202, 10.1038/nchembio.1202]
[7]   In-cell NMR in E. coli to Monitor Maturation Steps of hSOD1 [J].
Banci, Lucia ;
Barbieri, Letizia ;
Bertini, Ivano ;
Cantini, Francesca ;
Luchinat, Enrico .
PLOS ONE, 2011, 6 (08)
[8]   Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells [J].
Barbieri, Letizia ;
Luchinat, Enrico ;
Banci, Lucia .
NATURE PROTOCOLS, 2016, 11 (06) :1101-1111
[9]   Protein interaction patterns in different cellular environments are revealed by in-cell NMR [J].
Barbieri, Letizia ;
Luchinat, Enrico ;
Banci, Lucia .
SCIENTIFIC REPORTS, 2015, 5
[10]   Cryo-Electron Tomography: Can it Reveal the Molecular Sociology of Cells in Atomic Detail? [J].
Beck, Martin ;
Baumeister, Wolfgang .
TRENDS IN CELL BIOLOGY, 2016, 26 (11) :825-837
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