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Why some proteins can take the heat Chemists at the University of Georgia have determined how hydrogen bonding contributes to one protein’s ability to withstand high temperatures. Catherine M. Bougault, Marly K. Eidsness, and James H. Prestegard used NMR spectroscopy to compare hydrogen bonding in two different rubredoxin proteins, one isolated from a thermophilic microbe found in the ocean near an Italian volcano and the other from a bacterium that prefers more temperate locales [Biochemistry, published online March 28, http://dx.doi.org/10.1021/bi027264d]. They showed that a redistribution of hydrogen bonds to stabilize an important metal-binding site—and not an increase in the number of hydrogen bonds—accounts for the increased heat stability of the thermophilic rubredoxin. Although theoretical studies have shown that hydrogen bonding and other interactions can play a role in stabilizing thermophilic proteins, this is the first time scientists have been able to specifically assess the contribution of hydrogen bonding. Understanding why thermophilic proteins can stand the heat is critical for designing commercially useful enzymes that work at high temperatures, the authors note. |
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