Publication date: Available online 7 November 2017 Source:Progress in Nuclear Magnetic Resonance Spectroscopy
Author(s): Philip W. Kuchel, Kiaran Kirk, Dmitry Shishmarev
The physicochemical environment inside cells is distinctly different from that immediately outside. The selective exchange of water, ions, and molecules across the cell membrane, mediated by integral, membrane-embedded proteins is a hallmark of living systems. There are various methodologies available to measure the selectivity and rates (kinetics) of such exchange processes, including several that take advantage of the non-invasive nature of NMR spectroscopy. A number of solutes, including particular inorganic ions, show distinctive NMR behaviour, in which separate resonances arise from the intra- and extracellular solute populations, without the addition of shift reagents, differences in pH, or selective binding partners. This ‘split peak effect/phenomenon’, discovered in 1984, has become a valuable tool, used in many NMR studies of cellular behaviour and function. The explanation for the phenomenon, based on the differential hydrogen bonding of the reporter solutes to water, and the various ways in which this phenomenon has been used to investigate aspects of cellular biochemistry and physiology, are the topics of this review. Graphical abstract
[NMR paper] Membrane solid-state NMR in Canada: A historical perspective.
Membrane solid-state NMR in Canada: A historical perspective.
Related Articles Membrane solid-state NMR in Canada: A historical perspective.
Biochim Biophys Acta. 2017 Jun 23;:
Authors: Auger M
Abstract
This manuscript presents an overview of more than 40years of membrane solid-state nuclear magnetic resonance (NMR) research in Canada. This technique is a method of choice for the study of the structure and dynamics of lipid bilayers; bilayer interactions with a variety of molecules such as membrane peptides, membrane proteins and...
The Nuclear Overhauser Effect from a Quantitative Perspective
The Nuclear Overhauser Effect from a Quantitative Perspective
Publication date: Available online 22 November 2013
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Beat Vögeli</br>
The nuclear Overhauser enhancement or effect (NOE) is the most important measure in liquid-state NMR with macromolecules. Thus, the NOE is the subject of numerous reviews and books. Here, the NOE is revisited in light of our recently introduced measurements of exact nuclear Overhauser enhancements (eNOEs), which enabled the determination of multiple-state 3D...
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Interactionsof Bacterial Cell Division Protein FtsZwith C8-Substituted Guanine Nucleotide Inhibitors. A Combined NMR,Biochemical and Molecular Modeling Perspective
Interactionsof Bacterial Cell Division Protein FtsZwith C8-Substituted Guanine Nucleotide Inhibitors. A Combined NMR,Biochemical and Molecular Modeling Perspective
Filipa Marcelo, Sonia Huecas, Laura B. Ruiz-A?vila, F. Javier Can?ada, Almudena Perona, Ana Poveda, Sonsoles Marti?n-Santamari?a, Antonio Morreale, Jesu?s Jime?nez-Barbero and Jose? M. Andreu
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja405515r/aop/images/medium/ja-2013-05515r_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja405515r...
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[NMR paper] Interactions of bacterial cell division protein FtsZ with C8-substituted guanine nucleotide inhibitors. A combined NMR, biochemical and molecular modeling perspective.
Interactions of bacterial cell division protein FtsZ with C8-substituted guanine nucleotide inhibitors. A combined NMR, biochemical and molecular modeling perspective.
Interactions of bacterial cell division protein FtsZ with C8-substituted guanine nucleotide inhibitors. A combined NMR, biochemical and molecular modeling perspective.
J Am Chem Soc. 2013 Sep 30;
Authors: Marcelo F, Huecas S, Ruiz-Avila LB, Cañada FJ, Perona A, Poveda A, Martin-Santamaria S, Morreale A, Jimenez-Barbero J, Andreu JM
Abstract
FtsZ is the key protein of...
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[NMR images] NMR Experiment explanation is
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[NMR paper] 1H and 31P NMR and HPLC studies of mouse L1210 leukemia cell extracts: the effect of
1H and 31P NMR and HPLC studies of mouse L1210 leukemia cell extracts: the effect of Au(I) and Cu(I) diphosphine complexes on the cell metabolism.
Related Articles 1H and 31P NMR and HPLC studies of mouse L1210 leukemia cell extracts: the effect of Au(I) and Cu(I) diphosphine complexes on the cell metabolism.
Magn Reson Med. 1991 Mar;18(1):142-58
Authors: Berners-Price SJ, Sant ME, Christopherson RI, Kuchel PW
The effect of the antitumor complex Cl (where dppe is Ph2P(CH2)2PPh2) on the overall metabolism of cultured mouse L1210 leukemia cells...