How sheilding and deshielding affect peak position in nmr studies?
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Nuclear magnetic resonance spectroscopy is used to study the structure of molecules, the interaction of various molecules, the kinetics or dynamics of molecules and the composition of mixtures of biological or synthetic solutions or composites.
The size of the molecules analyzed can range from a small organic molecule or metabolite, to a mid-sized peptide or a natural product, all the way up to proteins of several tens of kDa in molecular weight.
NMR nuclear spectroscopy complements other structural and analytical techniques such as X-ray, crystallography and mass spectrometry. NMR’s advantage is the unique ability of a nuclear spectrometer to allow both the non-destructive and the quantitative study of molecules in solution and in solid state, as well as to enable the study of biological fluids
The size of the molecules analyzed can range from a small organic molecule or metabolite, to a mid-sized peptide or a natural product, all the way up to proteins of several tens of kDa in molecular weight.
NMR nuclear spectroscopy complements other structural and analytical techniques such as X-ray, crystallography and mass spectrometry. NMR’s advantage is the unique ability of a nuclear spectrometer to allow both the non-destructive and the quantitative study of molecules in solution and in solid state, as well as to enable the study of biological fluids
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