Not only did he excel in academic work, winning the 2002 Nobel Prize in Chemistry for his advancement
of nuclear magnetic resonance spectroscopy, but Wüthrich was also an avid sportsman.
In 1 sentence: PNNL scientists removed a limitation
of nuclear magnetic resonance spectroscopy to enable studies never before possible under the extreme conditions found in nature.
The technology brings together the power
of nuclear magnetic resonance spectroscopy, which yields a remarkable peek into molecular interactions, and the ability to re-create the extreme conditions found on the tundra, in the deep ocean, or underground — conditions relevant to some of the biggest questions that scientists at DOE laboratories such as PNNL ask.
This was made possible by a combination
of nuclear magnetic resonance spectroscopy (NMR) and electron paramagnetic resonance spectroscopy (EPR), two procedures that make it possible to characterise the structural configuration of a protein at atomic resolution.
Not exact matches
Although students at this level learn the basics
of techniques such as
nuclear magnetic resonance and infrared
spectroscopy in school, «they don't have the advantage
of using instruments,» Hewson points out.
To map the minute landscape
of molecules, at scales as tiny as just tenths
of a nanometer, and help decipher their functions, structural biologists have long relied on two tools:
nuclear magnetic resonance, or NMR,
spectroscopy and X-ray crystallography.
Using a technique called
nuclear magnetic resonance spectroscopy, the researchers measured the concentrations
of 21 metabolites key to nerve function in the brains
of 10 deceased schizophrenia patients and 12 normal human controls.
Why the drug combination works in resistant CML Why such a combination
of the two inhibitor types works in an animal model has now been explained by Prof. Stephan Grzesiek's team at the Biozentrum
of the University
of Basel and Dr. Wolfgang Jahnke from Novartis, by a structural analysis using
nuclear magnetic resonance spectroscopy (NMR).
The researchers then used an array
of analytical tools — including stool and urine analysis, flow cytometry, light microscopy,
nuclear magnetic resonance spectroscopy, and 16S rRNA analysis — to observe the wide - ranging effects
of this sequential co-infection.
My particular field
of expertise (or more correctly, least incompetence) was investigating interactions
of the lithium ion with erythrocytes using
nuclear magnetic resonance (NMR)
spectroscopy.
«Using advanced
nuclear magnetic resonance spectroscopy, we were able to provide an unprecedented view
of the internal structure
of the protein clumps that form in the disease, which we hope will one day lead to new therapies.»
When Cegelski and her colleagues used a technique called
nuclear magnetic resonance spectroscopy to analyze the biofilm around samples
of E. coli, the researchers got a surprise.
Using
nuclear magnetic resonance spectroscopy, two teams working with the Göttingen - based scientists Markus Zweckstetter and Stefan Becker have now shown the complex three - dimensional structure
of the protein «at work» in atomic detail.
In developing this idea, the team clarified the distribution
of protons and oxygen vacancies in Sc - doped BaZrO3 by combining
nuclear magnetic resonance spectroscopy and thermogravimetric analysis.
We used Fourier - transform ion cyclotron
resonance mass spectrometry and
nuclear magnetic resonance spectroscopy to show that a sulfilimine bond -LRB-- S = N --RRB- crosslinks hydroxylysine - 211 and methionine - 93
of adjoining protomers, a bond not previously found in biomolecules.
Unfortunately, nature is not always willing to easily part with its secrets, forcing scientists to rely on sophisticated imaging technology —
nuclear magnetic resonance (NMR)
spectroscopy or mass spectrometry, for example — to decipher the molecular formula
of newly discovered organic compounds so they can be replicated in the lab.
With the help
of the electrons
of the resulting nitrogen vacancy center, even smallest
magnetic fields can be detected with a resolution
of a few nanometers thanks to
nuclear magnetic resonance (NMR)
spectroscopy.
LiWang's structural biology lab uses
nuclear magnetic resonance (NMR)
spectroscopy, the parent technology for MRI, to study the protein structure and dynamics
of biological molecules and then uses the structures to gain insights into their function.
Using a variety
of methods, including
nuclear magnetic resonance spectroscopy, calorimetry and electron microscopy, the researchers evaluated the fibers» structural and mechanical characteristics.
He used infrared
spectroscopy to verify the presence
of water on precursor lead - oleates, and
nuclear magnetic resonance to show that the lead oleate acted as a drying agent, grabbing water out
of the solvent.
Unusually for such a project, the TSRI chemists analyzed the 3D atomic structure
of their template compound using X-ray crystallography as well as
nuclear magnetic resonance spectroscopy.
Determination
of structure - substance and substance - receptor relations with
nuclear magnetic resonance or x-ray
spectroscopy.
It also underscores the utility
of solid - state
nuclear magnetic resonance (NMR)
spectroscopy for imaging the structures
of proteins associated with prion diseases.
Investigations
of the fibril specimen by solid - state
nuclear magnetic resonance spectroscopy provided additional data to build the model and helped to validate the structure.
Researchers characterized the new battery's chemical interactions using a variety
of advanced instruments — including
nuclear magnetic resonance, Raman
spectroscopy, mass
spectroscopy and more — at EMSL, the Environmental Molecular Sciences Laboratory, a DOE Office
of Science national user facility at PNNL.
To see if their approach worked, the team examined the healed material using
nuclear magnetic resonance spectroscopy and other tools at PNNL's Physical Sciences Laboratory along with the helium ion microscope at EMSL, a U.S. Department
of Energy Office
of Science user facility.
«Probing the molecular architecture
of Arabidopsis thaliana secondary cell walls using two - and three - dimensional (13) C solid state
nuclear magnetic resonance spectroscopy»
Our experimental and theoretical analysis draws upon
nuclear magnetic resonance (NMR)
spectroscopy, a variety
of microscopy techniques such as transmission electron microscopy, computation tools such as the NWChem for high - performance computational chemistry as well as supercomputers, and other tools.
The stage was set for success, with a dynamic local GPCR community and access to crucial tools
of the trade —
nuclear magnetic resonance (NMR)
spectroscopy and electron microscopy (EM), not to mention the synchrotron in Grenoble.
Once at Yale, he immersed himself in
nuclear magnetic resonance (NMR)
spectroscopy, to investigate the structure and dynamics
of molecules.
Alain Destexhe, Research Director
of Unité de Neurosciences CNRS, Gif - sur - Yvette, France Bruno Weber, Professor
of Multimodal Experimental Imaging, Universitaet Zuerich, Switzerland Carmen Gruber Traub, Fraunhofer, Germany Costas Kiparissides, Certh, Greece Cyril Poupon, Head
of the
Nuclear Magnetic Resonance Imaging and
Spectroscopy unit
of NeuroSpin, University Paris Saclay, Gif - sur - Yvette, France David Boas, Professor
of Radiology at Massachusetts General Hospital, Harvard Medical School, University
of Pennsylvania Hanchuan Peng, Associate Investigator at Allen Brain Institute, Seattle, US Huib Manswelder, Head
of Department
of Integrative Neurophysiology Center for Neurogenomics and Cognitive Research, VU University, Amsterdam Jan G. Bjaalie, Head
of Neuroinformatics division, Institute
of Basic Medical Sciences, University
of Oslo, Norway Jean - François Mangin, Research Director Neuroimaging at CEA, Gif - sur - Yvette, France Jordi Mones, Institut de la Macula y la Retina, Barcelona, Spain Jurgen Popp, Scientific Director
of the Leibniz Institute
of Photonic Technology, Jena, Germany Katharina Zimmermann, Hochshule, Germany Katrin Amunts, Director
of the Institute Structural and functional organisation
of the brain, Forschungszentrum Juelich, Germany Leslie M. Loew, Professor at University
of Connecticut Health Center, Connecticut, US Marc - Oliver Gewaltig, Section Manager
of Neurorobotics, Simulation Neuroscience Division - Ecole Polytechnique fédérale de Lausanne (EPFL), Geneve, Switzerland Markus Axer, Head
of Fiber architecture group, Institute
of Neuroscience and Medicine (INM - 1) at Forschungszentrum Juelich, Germany Mickey Scheinowitz, Head
of Regenerative Therapy Department
of Biomedical Engineering and Neufeld Cardiac Research Institute, Tel - Aviv University, Israel Pablo Loza, Institute
of Photonic Sciences, Castelldefels, Spain Patrick Hof, Mount Sinai Hospital, New York, US Paul Tiesinga, Professor at Faculty
of Science, Radboud University, Nijmegen, Netherlands Silvestro Micera, Director
of the Translational Neural Engineering (TNE) Laboratory, and Associate Professor at the EPFL School
of Engineering and the Centre for Neuroprosthetics Timo Dicksheid, Group Leader
of Big Data Analytics, Institute Structural and functional organisation
of the brain, Forschungszentrum Juelich, Germany Trygve Leergaard, Professor
of Neural Systems, Institute
of Basic Medical Sciences, University
of Oslo, Norway Viktor Jirsa, Director
of the Institute de Neurosciences des Systèmes and Director
of Research at the CNRS, Marseille, France
Using
nuclear magnetic resonance (NMR)
spectroscopy, however, he found at least two different arrangements
of the two domains in the protein: one open, one closed, neither resembling that
of the crystal structure.
On the other hand, dynamic
nuclear polarization
of molecules via nitrogen vacancy centers has important applications in
nuclear magnetic resonance spectroscopy since it would greatly increase the standard sensitivity
of current scanners.
He'd found his way from the University
of Utrecht, in the Netherlands, where he'd done his PhD on
Nuclear Magnetic Resonance (NMR)
spectroscopy, to Uppsala, in Sweden, where as a young post-doc he was learning X-ray crystallography from Alwyn Jones.
Using
nuclear magnetic resonance (NMR)
spectroscopy, computer simulations and microscopy, the researchers showed how disease mutations and arginine methylation, a functional modification common to a large family
of proteins with low - complexity domains, altered the formation
of the liquid droplets and their conversion to solid - like states in disease.