Effect of Prostaglandin and Bisphosphonate on Cancellous Bone Volume and Structure in the Ovariectomized Rat Studied by Quantitative Three-Dimensional Nuclear Magnetic Resonance Microscopy

1999 ◽  
Vol 14 (5) ◽  
pp. 680-689 ◽  
Author(s):  
Masaya Takahashi ◽  
Felix W. Wehrli ◽  
Suzanne L. Wehrli ◽  
Scott N. Hwang ◽  
Mark W. Lundy ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Cancellous Bone ◽  
Three Dimensional ◽  
Bone Volume ◽  
Ovariectomized Rat ◽  
Magnetic Resonance Microscopy ◽  
Nuclear Magnetic

Voxel size effects in three-dimensional nuclear magnetic resonance microscopy performed for trabecular bone dosimetry

2000 ◽  
Vol 27 (11) ◽  
pp. 2624-2635 ◽  
Author(s):  
D. A. Rajon ◽  
D. W. Jokisch ◽  
P. W. Patton ◽  
A. P. Shah ◽  
W. E. Bolch
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Trabecular Bone ◽  
Size Effects ◽  
Three Dimensional ◽  
Magnetic Resonance Microscopy ◽  
Voxel Size ◽  
Nuclear Magnetic

Nuclear magnetic resonance microscopy with 4-μm resolution: Theoretical study and experimental results

1988 ◽  
Vol 15 (6) ◽  
pp. 815-824 ◽  
Author(s):  
Z. H. Cho ◽  
C. B. Ahn ◽  
S. C. Juh ◽  
H. K. Lee ◽  
R. E. Jacobs ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Theoretical Study ◽  
Experimental Results ◽  
Magnetic Resonance Microscopy ◽  
Nuclear Magnetic

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.

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
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