2brz: Difference between revisions

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[[Image:2brz.gif|left|200px]]<br /><applet load="2brz" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2brz.gif|left|200px]]<br /><applet load="2brz" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2brz" />

'''SOLUTION NMR STRUCTURE OF THE SWEET PROTEIN BRAZZEIN, MINIMIZED AVERAGE STRUCTURE'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pentadiplandra_brazzeana Pentadiplandra brazzeana]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2BRZ OCA].

2BRZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pentadiplandra_brazzeana Pentadiplandra brazzeana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BRZ OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Abildgaard, F.]]

[[Category: Caldwell, J.E.]]

[[Category: Caldwell, J E.]]

[[Category: Dzakula, Z.]]

[[Category: Hellekant, G.]]

[[Category: Markley, J.L.]]

[[Category: Markley, J L.]]

[[Category: Ming, D.]]

[[Category: cysteine-stabilized alpha-beta]]

[[Category: sweet protein]]

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@@ Line 1: / Line 1: @@
-[[Image:2brz.gif|left|200px]]<br /><applet load="2brz" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2brz.gif|left|200px]]<br /><applet load="2brz" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2brz" />
 '''SOLUTION NMR STRUCTURE OF THE SWEET PROTEIN BRAZZEIN, MINIMIZED AVERAGE STRUCTURE'''<br />
 ==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.
+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==
-BRZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pentadiplandra_brazzeana Pentadiplandra brazzeana]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BRZ OCA].
+BRZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pentadiplandra_brazzeana Pentadiplandra brazzeana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BRZ OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Abildgaard, F.]]
-[[Category: Caldwell, J.E.]]
+[[Category: Caldwell, J E.]]
 [[Category: Dzakula, Z.]]
 [[Category: Hellekant, G.]]
-[[Category: Markley, J.L.]]
+[[Category: Markley, J L.]]
 [[Category: Ming, D.]]
 [[Category: cysteine-stabilized alpha-beta]]
 [[Category: sweet protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:53:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:59 2008''