JMSSJ On-line, Vol. 48 (2000) No. 2, pp. 94-100
Probing the Higher Order Structure of Proteins by Hydrogen/Deuterium Exchange and Mass Spectrometry
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    Satoko AKASHI*a) and Koji TAKIOa)

    *a) Division of Biomolecular Characterization, RIKEN (The Institute of Physical and Chemical Research) (2-1 Hirosawa, Wako, 351-0198, Japan)

In order to understand the protein function in detail, it is important to have information on tertiary structure of the protein. Protein tertiary structure has generally been studied using X-ray crystallography and NMR. However, these techniques require a large scale sample preparation. On the other hand, mass spectrometry requires a smaller sample amount and is much faster than X-ray crystallography or NMR. These are great advantages of MS in the structural characterization of a protein. In the present commentary, it will be described how to study the tertiary structure of proteins using hydrogen-deuterium exchange in conjunction with mass spectrometry.

Key words: Protein structure, ESI, H/D exchange, FTICR MS

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