Plant storage proteins are resistant to proteolytic digestion. However, some limited regions of the poly-peptide-chains are nicked by protease attack. By the attack, the proteins change to digestion intermediates that have stable conformation. Similar phenomena have been also reported on in vitro digestion or in germination of several plant storage proteins. Therefore, the limited proteolysis is a common nature of plant storage proteins and may have important role in seed germination. The fragmentation sequence analysis combined with the computer prediction of the secondary and tertiary structure describes the detailed information on the soybean glycinin conformation. Recent progress on nucleic acid sequence studies on the plant storage proteins makes it possible to predict the evolution of the three dimentional structure of the proteins. These methods will be a useful way for describing conformation of a plant protein that has not been crystallized.
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