scholarly journals Nuclear Magnetic Resonance Spectroscopyan Evolutionary Approach to Drug Design

2007 ◽  
Vol 4 (3) ◽  
pp. 294-301
Author(s):  
Neeraj Upmanyu ◽  
Gopal Garg ◽  
Archana Dolly ◽  
Pradeep Mishra
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Drug Discovery ◽  
Magnetic Resonance ◽  
Drug Design ◽  
Small Molecules ◽  
Pharmaceutical Research ◽  
Three Dimensional ◽  
Drug Discovery And Development ◽  
4D Nmr ◽  
Nuclear Magnetic

Ever since Nuclear Magnetic Resonance (NMR) spectroscopy hit the analytical scene; its capabilities and applications continue to evolve. Originally designed as a way to verify the structure of relatively small compounds, the technology of NMR has exploded and become a valuable means for studying protein structure. NMR has proved to be a valuable tool in pharmaceutical research, as it has entered new arena of drug discovery and structural genomics. NMR can provide information on the three-dimensional structures of small molecules in solution, high-molecular-weight complexes, and the details of enzyme mechanisms that can be used to aid in drug design. In the present scenario, the availability of high magnetic fields; improved software, high resolution probes, and electronics; more versatile pulse programmers; and most importantly the development of 2D, 3D and 4D NMR, have revolutionized the field of drug discovery and development.

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
Sign in / Sign up

Export Citation Format

Share Document