Targeted using magnetic resonance

However, the determination of affinity does not necessarily have to rely on labeled ligands. It is also possible with native ligands when using suitable detection methods, as for example nuclear magnetic resonance (NMR), surface plasmon resonance (SPR), acoustic biosensors or calorimetry [48, 49]. A particularly versatile and sensitive detection principle for the investigation of interactions between targets and native ligands is mass spectrometry [50]. 

Until quite recently, X-ray crystallography was the technique used almost exclusively to resolve the 3-D structure of proteins. As well as itself being technically challenging, a major limitation of X-ray crystallography is the requirement for the target protein in crystalline form. It has thus far proved difficult or impossible to induce the majority of proteins to crystallize. Nuclear magnetic resonance (NMR) is an analytical technique which can also be used to determine the three-dimensional structure of a molecule without the necessity for crystallization. For many years, even the most powerful NMR machines could resolve the 3-D structure of only relatively small proteins (less than 20-25 kDa). However, recent analytical advances now render it possible to successfully analyse much larger proteins by this technique. 

Targeted particles for molecular imaging using US and magnetic resonance 466... 

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