NMR is of particular value as a non-destructive analytical method, with the demonstrated capacity to be used as a primary method for quantification, being able to tolerate a wide variety of hydrophilic and hydrophobic components within a given matrix and still allow for quantification and characterisation e.g. micellisation in the presence of surfactants. In this investigation we have undertaken steps to attain a trueness level <10%, repeatability values of <1% and the limit of quantitation down to 100nM (≈ limit of baseline range of Vitamin D2 and D3 per litre seen in vivo). Pure shift sequences are currently being implemented into our 1D and 2D experiments to allow for greater resolution when working with complex mixtures.
My interest for NMR developed during my undergraduate degree in Biochemistry, where I pursued this interest into a 8 week summer internship, working alongside researchers of the Wellcome trust NMR lab at the University of Kent, determining peptide structures through the use of NOESY and COSY, 2D NMR techniques used here for qualitative analysis of 8 different peptides related to the αv β6 integrin.
I further pursued my interest in magnetic resonance (MR) within the realms of chemical analysis and healthcare through my master's in Neuroimaging at King's College London. This allowed me to expand my knowledge of MR and build a strong physics background for MR, also understanding the versatility of this technique when tailored to a certain function.