2a3d

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==Overview==
==Overview==
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Although de novo protein design is an important endeavor with implications, for understanding protein folding, until now, structures have been, determined for only a few 25- to 30-residue designed miniproteins. Here, the NMR solution structure of a complex 73-residue three-helix bundle, protein, alpha3D, is reported. The structure of alpha3D was not based on, any natural protein, and yet it shows thermodynamic and spectroscopic, properties typical of native proteins. A variety of features contribute to, its unique structure, including electrostatics, the packing of a diverse, set of hydrophobic side chains, and a loop that incorporates common, capping motifs. Thus, it is now possible to design a complex protein with, a well defined and predictable three-dimensional structure.
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Although de novo protein design is an important endeavor with implications for understanding protein folding, until now, structures have been determined for only a few 25- to 30-residue designed miniproteins. Here, the NMR solution structure of a complex 73-residue three-helix bundle protein, alpha3D, is reported. The structure of alpha3D was not based on any natural protein, and yet it shows thermodynamic and spectroscopic properties typical of native proteins. A variety of features contribute to its unique structure, including electrostatics, the packing of a diverse set of hydrophobic side chains, and a loop that incorporates common capping motifs. Thus, it is now possible to design a complex protein with a well defined and predictable three-dimensional structure.
==About this Structure==
==About this Structure==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Bryson, J.W.]]
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[[Category: Bryson, J W.]]
[[Category: Cheng, H.]]
[[Category: Cheng, H.]]
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[[Category: Degrado, W.F.]]
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[[Category: Degrado, W F.]]
[[Category: Roder, H.]]
[[Category: Roder, H.]]
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[[Category: Walsh, S.T.R.]]
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[[Category: Walsh, S T.R.]]
[[Category: three-helix bundle]]
[[Category: three-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:13:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:12 2008''

Revision as of 14:23, 21 February 2008


2a3d

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SOLUTION STRUCTURE OF A DE NOVO DESIGNED SINGLE CHAIN THREE-HELIX BUNDLE (A3D)

Overview

Although de novo protein design is an important endeavor with implications for understanding protein folding, until now, structures have been determined for only a few 25- to 30-residue designed miniproteins. Here, the NMR solution structure of a complex 73-residue three-helix bundle protein, alpha3D, is reported. The structure of alpha3D was not based on any natural protein, and yet it shows thermodynamic and spectroscopic properties typical of native proteins. A variety of features contribute to its unique structure, including electrostatics, the packing of a diverse set of hydrophobic side chains, and a loop that incorporates common capping motifs. Thus, it is now possible to design a complex protein with a well defined and predictable three-dimensional structure.

About this Structure

2A3D is a Protein complex structure of sequences from Escherichia coli. The following page contains interesting information on the relation of 2A3D with [Designer Proteins]. Full crystallographic information is available from OCA.

Reference

Solution structure and dynamics of a de novo designed three-helix bundle protein., Walsh ST, Cheng H, Bryson JW, Roder H, DeGrado WF, Proc Natl Acad Sci U S A. 1999 May 11;96(10):5486-91. PMID:10318910

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