Live Cell NMR

被引:117
作者
Freedberg, Daron I. [1 ]
Selenko, Philipp [2 ]
机构
[1] USDA, Lab Bacterial Polysaccharides, Ctr Biol Evaluat & Res, Rockville, MD 20852 USA
[2] Leibniz Inst Mol Pharmacol FMP Berlin, Dept NMR Supported Struct Biol, In Cell NMR Lab, D-13125 Berlin, Germany
来源
ANNUAL REVIEW OF BIOPHYSICS, VOL 43 | 2014年 / 43卷
关键词
in-cell NMR; on-cell NMR; in-cell EPR; macromolecular crowding; excluded volume; soft interactions; SOLID-STATE NMR; DYNAMIC NUCLEAR-POLARIZATION; XENOPUS-LAEVIS OOCYTES; ANGLE-SPINNING NMR; MAGNETIC-RESONANCE-SPECTROSCOPY; PROTEIN-PROTEIN INTERACTIONS; LIVING MAMMALIAN-CELLS; IN-CELL; ESCHERICHIA-COLI; F-19; NMR;
D O I
10.1146/annurev-biophys-051013-023136
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Ever since scientists realized that cells are the basic building blocks of all life, they have been developing tools to look inside them to reveal the architectures and mechanisms that define their biological functions. Whereas "looking into cells" is typically said in reference to optical microscopy, high-resolution in-cell and on-cell nuclear magnetic resonance (NMR) spectroscopy is a powerful method that offers exciting new possibilities for structural and functional studies in and on live cells. In contrast to conventional imaging techniques, in-and on-cell NMR methods do not provide spatial information on cellular biomolecules. Instead, they enable atomic-resolution insights into the native cell states of proteins, nucleic acids, glycans, and lipids. Here we review recent advances and developments in both fields and discuss emerging concepts that have been delineated with these methods.
引用
收藏
页码:171 / 192
页数:22
相关论文
共 109 条
[61]   Adding New Chemistries to the Genetic Code [J].
Liu, Chang C. ;
Schultz, Peter G. .
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 79, 2010, 79 :413-444
[62]   Biased Signaling Pathways in β2-Adrenergic Receptor Characterized by 19F-NMR [J].
Liu, Jeffrey J. ;
Horst, Reto ;
Katritch, Vsevolod ;
Stevens, Raymond C. ;
Wuethrich, Kurt .
SCIENCE, 2012, 335 (6072) :1106-1110
[63]   In-cell NMR spectroscopy [J].
Maldonado, Andres Y. ;
Burz, David S. ;
Shekhtman, Alexander .
PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, 2011, 59 (03) :197-212
[64]   1D saturation transfer difference NMR experiments on living cells:: The DC-SIGN/oligomannose interaction [J].
Mari, S ;
Serrano-Gómez, D ;
Cañada, FJ ;
Corbí, AL ;
Jiménez-Barbera, J .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2005, 44 (02) :296-298
[65]   2D TR-NOESY Experiments Interrogate and Rank Ligand-Receptor Interactions in Living Human Cancer Cells [J].
Mari, Silvia ;
Invernizzi, Chiara ;
Spitaleri, Andrea ;
Alberici, Luca ;
Ghitti, Michela ;
Bordignon, Claudio ;
Traversari, Catia ;
Rizzardi, Gian-Paolo ;
Musco, Giovanna .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2010, 49 (06) :1071-1074
[66]   An upper limit for macromolecular crowding effects [J].
Miklos, Andrew C. ;
Li, Conggang ;
Sorrell, Courtney D. ;
Lyon, L. Andrew ;
Pielak, Gary J. .
BMC BIOPHYSICS, 2011, 4
[67]   Protein Crowding Tunes Protein Stability [J].
Miklos, Andrew C. ;
Sarkar, Mohona ;
Wang, Yaqiang ;
Pieak, Gary J. .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2011, 133 (18) :7116-7120
[68]   Volume Exclusion and Soft Interaction Effects on Protein Stability under Crowded Conditions [J].
Miklos, Andrew C. ;
Li, Conggang ;
Sharaf, Naima G. ;
Pielak, Gary J. .
BIOCHEMISTRY, 2010, 49 (33) :6984-6991
[69]   Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding [J].
Minton, Allen P. .
BIOPOLYMERS, 2013, 99 (04) :239-244
[70]   Implications of macromolecular crowding for protein assembly [J].
Minton, AP .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2000, 10 (01) :34-39