1gto: Difference between revisions

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

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

caption="1gto, resolution 1.82Å" />

'''HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT'''<br />

==Overview==

A surface turn position in a four-helix bundle protein, Rop, was selected, to investigate the role of turns in protein structure and stability., Although all twenty amino acids can be substituted at this position to, generate a correctly folded protein, they produce an unusually large range, of thermodynamic stabilities. Moreover, the majority of substitutions give, rise to proteins with enhanced thermal stability compared to that of the, wild type. By introducing the same twenty mutations at this position, but, in a simplified context, we were able to deconvolute intrinsic preferences, from local environmental effects. The intrinsic preferences can be, explained on the basis of preferred backbone dihedral angles, but local, environmental context can significantly modify these effects.

A surface turn position in a four-helix bundle protein, Rop, was selected to investigate the role of turns in protein structure and stability. Although all twenty amino acids can be substituted at this position to generate a correctly folded protein, they produce an unusually large range of thermodynamic stabilities. Moreover, the majority of substitutions give rise to proteins with enhanced thermal stability compared to that of the wild type. By introducing the same twenty mutations at this position, but in a simplified context, we were able to deconvolute intrinsic preferences from local environmental effects. The intrinsic preferences can be explained on the basis of preferred backbone dihedral angles, but local environmental context can significantly modify these effects.

==About this Structure==

1GTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1GTO OCA].

1GTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTO OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Agrawal, V.]]

[[Category: Brunger, A.T.]]

[[Category: Brunger, A T.]]

[[Category: Predki, P.]]

[[Category: Regan, L.]]

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[[Category: turn]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 16~~:17:~~05 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:03 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1gto.gif|left|200px]]<br /><applet load="1gto" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1gto.gif|left|200px]]<br /><applet load="1gto" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1gto, resolution 1.82&Aring;" />
 '''HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT'''<br />
 ==Overview==
-A surface turn position in a four-helix bundle protein, Rop, was selected, to investigate the role of turns in protein structure and stability., Although all twenty amino acids can be substituted at this position to, generate a correctly folded protein, they produce an unusually large range, of thermodynamic stabilities. Moreover, the majority of substitutions give, rise to proteins with enhanced thermal stability compared to that of the, wild type. By introducing the same twenty mutations at this position, but, in a simplified context, we were able to deconvolute intrinsic preferences, from local environmental effects. The intrinsic preferences can be, explained on the basis of preferred backbone dihedral angles, but local, environmental context can significantly modify these effects.
+A surface turn position in a four-helix bundle protein, Rop, was selected to investigate the role of turns in protein structure and stability. Although all twenty amino acids can be substituted at this position to generate a correctly folded protein, they produce an unusually large range of thermodynamic stabilities. Moreover, the majority of substitutions give rise to proteins with enhanced thermal stability compared to that of the wild type. By introducing the same twenty mutations at this position, but in a simplified context, we were able to deconvolute intrinsic preferences from local environmental effects. The intrinsic preferences can be explained on the basis of preferred backbone dihedral angles, but local environmental context can significantly modify these effects.
 ==About this Structure==
-GTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTO OCA].
+GTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTO OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Agrawal, V.]]
-[[Category: Brunger, A.T.]]
+[[Category: Brunger, A T.]]
 [[Category: Predki, P.]]
 [[Category: Regan, L.]]
@@ Line 22: / Line 22: @@
 [[Category: turn]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:17:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:03 2008''