Search results
Results from the WOW.Com Content Network
Carbohydrate NMR spectroscopy is the application of nuclear magnetic resonance (NMR) spectroscopy to structural and conformational analysis of carbohydrates.This method allows the scientists to elucidate structure of monosaccharides, oligosaccharides, polysaccharides, glycoconjugates and other carbohydrate derivatives from synthetic and natural sources.
(Techniques have also been devised for generating heteronuclear correlation spectra, in which the two axes correspond to different isotopes, such as 13 C and 1 H.) Diagonal peaks correspond to the peaks in a 1D-NMR experiment, while the cross peaks indicate couplings between pairs of nuclei (much as multiplet splitting indicates couplings in 1D ...
The “dipole coupling”-based approach parallels protein NMR spectroscopy to some extent in that e.g. multiple residual dipolar couplings are measured for proteins in solution, and these couplings are used as constraints in the protein structure calculation. In NMR crystallography the observed spins in case of organic molecules would often be ...
Nuclear magnetic resonance decoupling (NMR decoupling for short) is a special method used in nuclear magnetic resonance (NMR) spectroscopy where a sample to be analyzed is irradiated at a certain frequency or frequency range to eliminate or partially the effect of coupling between certain nuclei. NMR coupling refers to the effect of nuclei on ...
Some of the most useful information for structure determination in a one-dimensional NMR spectrum comes from J-coupling, or scalar coupling (a special case of spin–spin coupling), between NMR active nuclei. This coupling arises from the interaction of different spin states through the chemical bonds of a molecule and results in the splitting ...
The coupling constants then differ because of geometry (cis vs. trans) or connectivity (2-bond vs. 3-bond) and the level of complexity will depend on the differences. Conformational dynamics may reduce or even obliterate the difference between cis and trans couplings, if fast compared to the NMR timescale. There may also be additional couplings ...
Most NMR studies of protein structure are based on analysis of the Nuclear Overhauser effect, NOE, between different protons in the protein. Because the NOE depends on the inverted sixth power of the distance between the nuclei, r −6 , NOEs can be converted into distance restraints that can be used in molecular dynamics -type structure ...
The notation labels each (NMR active) nucleus with a letter of the alphabet. The difference in chemical shift, δ, relative to the J-coupling between nuclei mirrors the separation of the letter labels in the Latin alphabet. The letters used tend to be limited to A,B,M,N,X,Y.