Nuclear Magnetic Resonance (NMR) is used in protein product characterisation to analyse the chemical structure and composition of biological molecules, including proteins, oligosaccharides, nucleic acids etc. NMR spectroscopy also provides insight into the three-dimensional structure of molecules, which is particularly useful in assessing the conformational integrity of protein-based therapeutics. It is frequently used as a method of comparing a sample with a known published product. NMR may be the only means of obtaining high resolution data on intrinsically unstructured proteins.
M-Scan has available research-level analysis on two biologically equipped 500MHz and 800 MHz shielded NMR spectrometers, with cryoprobe technology, providing some of the most sensitive instrumentation available.
The ICH Q6B guidelines, for characterisation and confirmation of biopharmaceuticals in support of new marketing applications, require Spectroscopic Profiling as part of the assessment of physicochemical properties of a product. The guidelines state that, "The ultraviolet and visible absorption spectra are determined as appropriate. The higher-order structure of the product is examined using procedures such as circular dichroism, nuclear magnetic resonance (NMR) or other suitable techniques, as appropriate".
M-Scan also offers GLP-level Circular Dichroism for spectroscopic profiling.
M-Scan Brochure: Biotechnology and Pharmaceutical Analysis (8pp.)