Abstract
MALDI-MS (matrix assisted laser desorption ionization mass spectrometry) may become a powerful tool in biochemistry in view of its accurate measurement of molecular mass of protein up to and above 300,000 Da (1). Noncovalent protein-protein interactions and subunit composition of protein multimers are the basis of molecular recognition and function in the biological world. As a result, detection of complex structure is an important problem. Conventional biochemical techniques used to detect noncovalent protein complexes include nondenaturing gel electrophoresis and size exclusion chromatography, which are useful in many cases, although neither determines molecular weight with accuracy.
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Bloom, B.R., Iden, C.R., Mastrangelo, I.A. (1998). Non-Covalent Hetero- and Homo-Oligomeric Protein Complexes Reassociate Differentially during MALDI-MS Analysis. In: Ens, W., Standing, K.G., Chernushevich, I.V. (eds) New Methods for the Study of Biomolecular Complexes. NATO ASI Series, vol 510. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-9046-4_17
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DOI: https://doi.org/10.1007/978-94-015-9046-4_17
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