Abstract
Diffusion-weighted spectroscopy is a unique tool for exploring the intracellular microenvironment in vivo. In living systems, diffusion may be anisotropic, when biological membranes exhibit particular orientation patterns. In this work, a volume selective diffusion-weighted sequence is proposed, allowing single-shot measurement of the trace of the diffusion tensor, which does not depend on tissue anisotropy. With this sequence, the minimal echo time is only three times the diffusion time. In addition, cross-terms between diffusion gradients and other gradients are cancelled out. An adiabatic version, similar to localization by adiabatic selective refocusing sequence, is then derived, providing partial immunity against cross-terms. Proof of concept is performed ex vivo on chicken skeletal muscle by varying tissue orientation and intra-voxel shim. In vivo performance of the sequence is finally illustrated in a U87 glioblastoma mouse model, allowing the measurement of the trace apparent diffusion coefficient for six metabolites, including J-modulated metabolites. Although measurement performed along three separate orthogonal directions would bring similar accuracy on trace apparent diffusion coefficient under ideal conditions, the method described here should be useful for probing intimate properties of the cells with minimal experimental bias.
Single-shot NMR measurement of protein unfolding landscapes
Single-shot NMR measurement of protein unfolding landscapes
June 2012
Publication year: 2012
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Volume 1824, Issue 6</br>
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The transient unfolding events from the native state of a protein towards higher energy states can be closely investigated by studying the process of hydrogen exchange. Here, we present BLUU-Tramp (Biophysics Laboratory University of Udine—Temperature ramp), a new method to measure the rates for the exchange process and the underlying equilibrium thermodynamic parameters, using...
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Li Ion Diffusion in the Anode Material Li12Si7: Ultrafast Quasi-1D Diffusion and Two Distinct Fast 3D Jump Processes Separately Revealed by 7Li NMR Relaxometry
Li Ion Diffusion in the Anode Material Li12Si7: Ultrafast Quasi-1D Diffusion and Two Distinct Fast 3D Jump Processes Separately Revealed by 7Li NMR Relaxometry
Alexander Kuhn, Puravankara Sreeraj, Rainer Po?ttgen, Hans-Dieter Wiemho?fer, Martin Wilkening and Paul Heitjans
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2020108/aop/images/medium/ja-2011-020108_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2020108
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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06-28-2011 04:32 AM
Postdoc Diffusion NMR
Postdoc Diffusion NMR
A position for a Project Scientist is available in the Knowledge Centre for Materials Chemistry (KCMC, http://www.materialschemistry.org) at the University of Manchester. The role is focused on the development and delivery of a capability to use diffusion NMR to investigate the dynamic behaviour of colloids and nanomaterials in aqueous dispersions. This work would be done in collaboration with external sponsors including industry, charities and research councils.
Candidates should hold a PhD in chemistry or materials science, and a strong research track record in...
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03-23-2011 07:41 PM
Spin Diffusion Driven by R-Symmetry Sequences: Applications to Homonuclear Correlation Spectroscopy in MAS NMR of Biological and Organic Solids.
Spin Diffusion Driven by R-Symmetry Sequences: Applications to Homonuclear Correlation Spectroscopy in MAS NMR of Biological and Organic Solids.
Spin Diffusion Driven by R-Symmetry Sequences: Applications to Homonuclear Correlation Spectroscopy in MAS NMR of Biological and Organic Solids.
J Am Chem Soc. 2011 Mar 1;
Authors: Hou G, Yan S, Sun S, Han Y, Byeon IJ, Ahn J, Concel J, Samoson A, Gronenborn AM, Polenova T
We present a family of homonuclear (13)C-(13)Cmagic angle spinning spin diffusion experiments, based on R2(n)(v) (n = 1 and 2, v = 1...
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03-03-2011 12:34 PM
Spin Diffusion Driven by R-Symmetry Sequences: Applications to Homonuclear Correlation Spectroscopy in MAS NMR of Biological and Organic Solids
Spin Diffusion Driven by R-Symmetry Sequences: Applications to Homonuclear Correlation Spectroscopy in MAS NMR of Biological and Organic Solids
Guangjin Hou, Si Yan, Shangjin Sun, Yun Han, In-Ja L. Byeon, Jinwoo Ahn, Jason Concel, Ago Samoson, Angela M. Gronenborn and Tatyana Polenova
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja108650x/aop/images/medium/ja-2010-08650x_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja108650x
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03-02-2011 02:01 AM
[NMR paper] Diffusion NMR spectroscopy: folding and aggregation of domains in p53.
Diffusion NMR spectroscopy: folding and aggregation of domains in p53.
Related Articles Diffusion NMR spectroscopy: folding and aggregation of domains in p53.
Chembiochem. 2005 Sep;6(9):1550-65
Authors: Dehner A, Kessler H
Protein interactions and aggregation phenomena are probably amongst the most ubiquitous types of interactions in biological systems; they play a key role in many cellular processes. The ability to identify weak intermolecular interactions is a unique feature of NMR spectroscopy. In recent years, pulsed-field gradient NMR...
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12-01-2010 06:56 PM
[Stan NMR blog] Free info about Diffusion and NMR
Free info about Diffusion and NMR
Proceedings of the 9th MRPM conference are now available for free in Diffusion Fundamentals.
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