Three-Dimensional Display Of Nuclear Magnetic Resonance Images

1982 ◽  
Vol 21 (5) ◽  
Author(s):  
Gabor T. Herman ◽  
David M. Kramer ◽  
Paul C. Lauterbur ◽  
Andrew M. Rudin ◽  
Jay S. Schneider
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Three Dimensional ◽  
Magnetic Resonance Images ◽  
Three Dimensional Display ◽  
Nuclear Magnetic

Three-Dimensional Display Of Nuclear Magnetic Resonance Images

1981 ◽  
Author(s):  
Gabor T. Herman ◽  
Jayaram K. Udupa ◽  
David M. Kramer ◽  
Paul C. Lauterbur ◽  
Andrew M. Rudin ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Three Dimensional ◽  
Magnetic Resonance Images ◽  
Three Dimensional Display ◽  
Nuclear Magnetic

Three-Dimensional Display of Nuclear Magnetic Resonance (NMR) Cardiovascular Images

1983 ◽  
Vol 7 (1) ◽  
pp. 172-174 ◽  
Author(s):  
Leon Axel ◽  
Gabor T. Herman ◽  
Jayaram K. Udupa ◽  
Paul A. Bottomley ◽  
William A. Edelstein
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Three Dimensional ◽  
Three Dimensional Display ◽  
Nuclear Magnetic

An emerging technology: Nuclear magnetic resonance microscopy

1988 ◽  
Vol 46 ◽  
pp. 1000-1001
Author(s):  
M.J. Hennessy ◽  
E. Kwok
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Relaxation Times ◽  
Basic Research ◽  
Local Environment ◽  
Magnetic Resonance Images ◽  
Nmr Microscopy ◽  
Mri Scans ◽  
Temperature Relaxation ◽  
Nuclear Magnetic

Much progress in nuclear magnetic resonance microscope has been made in the last few years as a result of improved instrumentation and techniques being made available through basic research in magnetic resonance imaging (MRI) technologies for medicine. Nuclear magnetic resonance (NMR) was first observed in the hydrogen nucleus in water by Bloch, Purcell and Pound over 40 years ago. Today, in medicine, virtually all commercial MRI scans are made of water bound in tissue. This is also true for NMR microscopy, which has focussed mainly on biological applications. The reason water is the favored molecule for NMR is because water is,the most abundant molecule in biology. It is also the most NMR sensitive having the largest nuclear magnetic moment and having reasonable room temperature relaxation times (from 10 ms to 3 sec). The contrast seen in magnetic resonance images is due mostly to distribution of water relaxation times in sample which are extremely sensitive to the local environment.

scholarly journals The Ensemble of Conformations of Antifreeze Glycoproteins (AFGP8): A Study Using Nuclear Magnetic Resonance Spectroscopy

Biomolecules ◽  
2019 ◽  
Vol 9 (6) ◽  
pp. 235
Author(s):  
Cheenou Her ◽  
Yin Yeh ◽  
Viswanathan V. Krishnan
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Three Dimensional ◽  
Random Coil ◽  
The Arctic ◽  
Native Structure ◽  
Antifreeze Glycoproteins ◽  
Structural Motifs ◽  
Ice Surface ◽  
Nuclear Magnetic

The primary sequence of antifreeze glycoproteins (AFGPs) is highly degenerate, consisting of multiple repeats of the same tripeptide, Ala–Ala–Thr*, in which Thr* is a glycosylated threonine with the disaccharide beta-d-galactosyl-(1,3)-alpha-N-acetyl-d-galactosamine. AFGPs seem to function as intrinsically disordered proteins, presenting challenges in determining their native structure. In this work, a different approach was used to elucidate the three-dimensional structure of AFGP8 from the Arctic cod Boreogadus saida and the Antarctic notothenioid Trematomus borchgrevinki. Dimethyl sulfoxide (DMSO), a non-native solvent, was used to make AFGP8 less dynamic in solution. Interestingly, DMSO induced a non-native structure, which could be determined via nuclear magnetic resonance (NMR) spectroscopy. The overall three-dimensional structures of the two AFGP8s from two different natural sources were different from a random coil ensemble, but their “compactness” was very similar, as deduced from NMR measurements. In addition to their similar compactness, the conserved motifs, Ala–Thr*–Pro–Ala and Ala–Thr*–Ala–Ala, present in both AFGP8s, seemed to have very similar three-dimensional structures, leading to a refined definition of local structural motifs. These local structural motifs allowed AFGPs to be considered functioning as effectors, making a transition from disordered to ordered upon binding to the ice surface. In addition, AFGPs could act as dynamic linkers, whereby a short segment folds into a structural motif, while the rest of the AFGPs could still be disordered, thus simultaneously interacting with bulk water molecules and the ice surface, preventing ice crystal growth.

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