cisandtransConfigurations of the Peptide Bond in N-Monosubstituted Amides by Nuclear Magnetic Resonance

1964 ◽  
Vol 86 (3) ◽  
pp. 337-341 ◽  
Author(s):  
Laurine A. LaPlanche ◽  
Max T. Rogers
2005 ◽  
Vol 348 (2) ◽  
pp. 383-397 ◽  
Author(s):  
Atsushi Kameda ◽  
Masaru Hoshino ◽  
Takashi Higurashi ◽  
Satoshi Takahashi ◽  
Hironobu Naiki ◽  
...  

1985 ◽  
Vol 63 (11) ◽  
pp. 3089-3101 ◽  
Author(s):  
Gilles Sauvé ◽  
Vanga S. Rao ◽  
Gilles Lajoie ◽  
Bernard Belleau

Reaction conditions for the synthesis of thioamide, amidoxime, and N-substituted amidine analogs of the peptide bond are described. Several new amidine analogs of the chemotactic peptide f-Met-Leu-Phe-OR were synthesized using the thioamides as precursors. The assignment of the E/Z configuration was accomplished by nuclear magnetic resonance. The biological activity of these analogs is briefly described.


Author(s):  
M.J. Hennessy ◽  
E. Kwok

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.


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