Structural highlights
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Walsh ST, Cheng H, Bryson JW, Roder H, DeGrado WF. Solution structure and dynamics of a de novo designed three-helix bundle protein. Proc Natl Acad Sci U S A. 1999 May 11;96(10):5486-91. PMID:10318910
