2a3d
SOLUTION STRUCTURE OF A DE NOVO DESIGNED SINGLE CHAIN THREE-HELIX BUNDLE (A3D)
OverviewOverview
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 StructureAbout this Structure
The following page contains interesting information on the relation of 2A3D with [Designer Proteins]. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 18:33:01 2008