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Research Article

ScienceAsia 24 (1998): 101-122 |doi: 10.2306/scienceasia1513-1874.1998.24.101



ABSTRACT: Now it is possible to determine the three-dimensional structure of paramagnetic proteins in solution through the state-of-the-art NMR techniques. The paramagnetic effects enhance the nuclear relaxation rate giving rise to undetectable NMR signals, thus NMR study of paramagnetic systems has been ignored. Nevertheless, such systems have been continuously studied by some NMR communities to eventually show that in a favorable ease, the problems can be overcome. The strategy to determine the structure of paramagnetic metalloproteins will be presented together with the highlights of data used for determining the three-dimensional structure of high-potential iron-sulfur proteins (HiPIPs) and ferricytochrome c. The strategy consists of the NMR conventional approach and an approach to paramagnetic systems. The quality of the structures determined is comparable to that of the diamagnetic proteins of the same size.

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Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand

Received May 18, 1998