1k09: Difference between revisions

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[[Image:1k09.jpg|left|200px]]<br /><applet load="1k09" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1k09.jpg|left|200px]]<br /><applet load="1k09" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1k09" />

'''Solution structure of BetaCore, A Designed Water Soluble Four-Stranded Antiparallel b-sheet Protein'''<br />

==Overview==

BetaCore is a designed approximately 50-residue protein in which two, BPTI-derived core modules, CM I and CM II, are connected by a 22-atom, cross-link. At low temperature and pH 3, homo- and heteronuclear NMR data, report a dominant folded ('f') conformation with well-dispersed chemical, shifts, i, i+1 periodicity, numerous long-range NOEs, and slowed amide, hydrogen isotope exchange patterns that is a four-stranded antiparallel, beta-sheet with nonsymmetrical and specific association of CM I and CM II., BetaCore 'f' conformations undergo reversible, global, moderately, cooperative, non-two-state thermal transitions to an equilibrium ensemble, of unfolded 'u' conformations. There is a significant energy barrier, between 'f' and 'u' conformations. This is the first designed, four-stranded antiparallel beta-sheet that folds in water.

BetaCore is a designed approximately 50-residue protein in which two BPTI-derived core modules, CM I and CM II, are connected by a 22-atom cross-link. At low temperature and pH 3, homo- and heteronuclear NMR data report a dominant folded ('f') conformation with well-dispersed chemical shifts, i, i+1 periodicity, numerous long-range NOEs, and slowed amide hydrogen isotope exchange patterns that is a four-stranded antiparallel beta-sheet with nonsymmetrical and specific association of CM I and CM II. BetaCore 'f' conformations undergo reversible, global, moderately cooperative, non-two-state thermal transitions to an equilibrium ensemble of unfolded 'u' conformations. There is a significant energy barrier between 'f' and 'u' conformations. This is the first designed four-stranded antiparallel beta-sheet that folds in water.

==About this Structure==

1K09 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1K09 OCA].

1K09 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K09 OCA].

==Reference==

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[[Category: four-stranded antiparallel beta-sheet]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 18~~:44:~~36 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:42 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1k09.jpg|left|200px]]<br /><applet load="1k09" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1k09.jpg|left|200px]]<br /><applet load="1k09" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1k09" />
 '''Solution structure of BetaCore, A Designed Water Soluble Four-Stranded Antiparallel b-sheet Protein'''<br />
 ==Overview==
-BetaCore is a designed approximately 50-residue protein in which two, BPTI-derived core modules, CM I and CM II, are connected by a 22-atom, cross-link. At low temperature and pH 3, homo- and heteronuclear NMR data, report a dominant folded ('f') conformation with well-dispersed chemical, shifts, i, i+1 periodicity, numerous long-range NOEs, and slowed amide, hydrogen isotope exchange patterns that is a four-stranded antiparallel, beta-sheet with nonsymmetrical and specific association of CM I and CM II., BetaCore 'f' conformations undergo reversible, global, moderately, cooperative, non-two-state thermal transitions to an equilibrium ensemble, of unfolded 'u' conformations. There is a significant energy barrier, between 'f' and 'u' conformations. This is the first designed, four-stranded antiparallel beta-sheet that folds in water.
+BetaCore is a designed approximately 50-residue protein in which two BPTI-derived core modules, CM I and CM II, are connected by a 22-atom cross-link. At low temperature and pH 3, homo- and heteronuclear NMR data report a dominant folded ('f') conformation with well-dispersed chemical shifts, i, i+1 periodicity, numerous long-range NOEs, and slowed amide hydrogen isotope exchange patterns that is a four-stranded antiparallel beta-sheet with nonsymmetrical and specific association of CM I and CM II. BetaCore 'f' conformations undergo reversible, global, moderately cooperative, non-two-state thermal transitions to an equilibrium ensemble of unfolded 'u' conformations. There is a significant energy barrier between 'f' and 'u' conformations. This is the first designed four-stranded antiparallel beta-sheet that folds in water.
 ==About this Structure==
-K09 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K09 OCA].
+K09 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K09 OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: four-stranded antiparallel beta-sheet]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:44:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:42 2008''