2brz
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(New page: 200px<br /><applet load="2brz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2brz" /> '''SOLUTION NMR STRUCTURE OF THE SWEET PROTEIN ...)
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Revision as of 06:46, 21 November 2007
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SOLUTION NMR STRUCTURE OF THE SWEET PROTEIN BRAZZEIN, MINIMIZED AVERAGE STRUCTURE
Overview
The fruit of Pentadiplandra brazzeana Baillon contains a small, sweet-tasting protein named brazzein. The structure of brazzein in, solution was determined by proton nuclear magnetic resonance spectroscopy, at pH 5.2 and 22 degrees C. The brazzein fold, which contains one, alpha-helix and three strands of antiparallel beta-sheet, does not, resemble that of either of the other two sweet-tasting proteins with known, structures, monellin and thaumatin. Instead, the structure of brazzein, resembles those of plant gamma-thionins and defensins and arthropod, toxins. Sequence comparisons predict that members of a newly-identified, family of serine proteinase inhibitors share the brazzein fold.
About this Structure
2BRZ is a Single protein structure of sequence from Pentadiplandra brazzeana. Full crystallographic information is available from OCA.
Reference
Solution structure of the thermostable sweet-tasting protein brazzein., Caldwell JE, Abildgaard F, Dzakula Z, Ming D, Hellekant G, Markley JL, Nat Struct Biol. 1998 Jun;5(6):427-31. PMID:9628478
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