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Walsh STR , Cheng H , Bryson JW , Roder H , DeGrado WF
Solution structure and dynamics of a de novo designed three- helix bundle protein
Proceedings of the National Academy of Sciences of the United States of America. 1999 May 11;96(10) :5486-5491
PMID: ISI:000080246500032   
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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. Acre, the NMR solution structure of a complex 73-residue three-helix bundle protein, alpha(3)D, is reported. The structure of alpha(3)D 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.
Times Cited: 39 English Article 195JG PROC NAT ACAD SCI USA