Publication date: Available online 3 June 2017 Source:Progress in Nuclear Magnetic Resonance Spectroscopy
Author(s): Arnab Mukherjee, Hunter C. Davis, Pradeep Ramesh, George J. Lu, Mikhail G. Shapiro
Magnetic resonance imaging (MRI) is a powerful technique for observing the function of specific cells and molecules inside living organisms. However, compared to optical microscopy, in which fluorescent protein reporters are available to visualize hundreds of cellular functions ranging from gene expression and chemical signaling to biomechanics, to date relatively few such reporters are available for MRI. Efforts to develop MRI-detectable biomolecules have mainly focused on proteins containing or transporting paramagnetic metals for T1 and T2 relaxation enhancement or large numbers of exchangeable protons for chemical exchange saturation transfer. While these pioneering developments established several key uses of biomolecular MRI, such as imaging of gene expression and functional biosensing, they also revealed that low molecular sensitivity poses a major challenge for broader adoption in biology and medicine. Recently, new classes of biomolecular reporters have been developed based on alternative contrast mechanisms, including enhancement of spin diffusivity, interactions with hyperpolarized nuclei, and modulation of blood flow. These novel reporters promise to improve sensitivity and enable new forms of multiplexed and functional imaging. Graphical abstract
[NMR paper] Access to aliphatic protons as reporters in non-deuterated proteins by solid-state NMR.
Access to aliphatic protons as reporters in non-deuterated proteins by solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Access to aliphatic protons as reporters in non-deuterated proteins by solid-state NMR.
Phys Chem Chem Phys. 2015 Dec 21;
Authors: Vasa SK, Rovó P, Giller K, Becker S, Linser R
Abstract
Interactions within proteins, with their surrounding, and with other molecules are mediated mostly by hydrogen atoms. In...
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Journal club
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12-28-2015 12:26 AM
[Question from NMRWiki Q&A forum] Total t1 evolution time, TROSY, PRE distance calculation
Total t1 evolution time, TROSY, PRE distance calculation
Hi all,
This is my first post to the forum and I am admittedly new to the field of protein NMR. I appreciate your patience with what could be a very rudimentary or simplistic question.
We have been trying to find the value for 'total INEPT evolution time' of the TROSY we ran for PRE distance calculations. We have everything worked out except that value which will give small changes to the R2 contribution from the spin label (R2spin). Im pretty sure its my incremental delay (in0) multiplied by the number of experiments (TD=512)....
nmrlearner
News from other NMR forums
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03-12-2014 01:10 AM
Site-Specific Spectroscopic Reporters
Site-Specific Spectroscopic Reporters
Provide a brief idea on how site specific labeling to understand protein properties.
More...
nmrlearner
General
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05-10-2013 06:58 AM
Studies of the Di-iron(VI)Intermediate in Ferrate-DependentOxygen Evolution from Water
Studies of the Di-iron(VI)Intermediate in Ferrate-DependentOxygen Evolution from Water
Rupam Sarma, Alfredo M. Angeles-Boza, David W. Brinkley and Justine P. Roth
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja304786s/aop/images/medium/ja-2012-04786s_0014.gif
Journal of the American Chemical Society
DOI: 10.1021/ja304786s
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/PQCNmRlTSgE
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09-06-2012 04:08 AM
[NMR paper] Signal identification in NMR spectra with coupled evolution periods.
Signal identification in NMR spectra with coupled evolution periods.
Related Articles Signal identification in NMR spectra with coupled evolution periods.
J Magn Reson. 2005 Sep;176(1):47-53
Authors: Malmodin D, Billeter M
Novel multidimensional NMR experiments rely on modified time-domain sampling schemes to provide significant savings of experimental time. Several approaches are based on the coupling of evolution times resulting in a reduction of the dimensionality of the recorded spectra, and a concomitant saving of experimental time. We...
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12-01-2010 06:56 PM
[NMR paper] Fast multidimensional NMR: radial sampling of evolution space.
Fast multidimensional NMR: radial sampling of evolution space.
Related Articles Fast multidimensional NMR: radial sampling of evolution space.
J Magn Reson. 2005 Apr;173(2):317-21
Authors: Kupce E, Freeman R
Multidimensional NMR spectroscopy can be speeded up by limited radial sampling of the time-domain evolution data. The resulting frequency-domain projections are used to reconstruct the full NMR spectrum. New algorithms are proposed to suppress back-projection artifacts while retaining optimum sensitivity. The method is illustrated by...
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11-25-2010 08:21 PM
How to process ZQ evolution in the indirect dimension
I want process ZQ evolution in the indirect dimension.
In Professor Pervushin's paper(Proc. Natl. Acad. Sci. USA
Vol. 96, pp. 9607–9612, August 1999). He has mentioned "After Fourier transformation in the w2 dimension, the
complex interferogram is multiplied by exp, where wh is the
offset in the w2 dimension relative to the 1H carrier frequency in rad/s."
Can anyone tell me the detail.
Biomolecular MRI Reporters: evolution of new mechanisms
Linear Mode
