Solution structure and dynamics of a de novo designed three-helix bundle protein.

Abstract:

: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.

authors

Walsh ST,Cheng H,Bryson JW,Roder H,DeGrado WF

doi

10.1073/pnas.96.10.5486

keywords:

subject

Has Abstract

pub_date

1999-05-11 00:00:00

pages

5486-91

issue

10

eissn

0027-8424

issn

1091-6490

journal_volume

96

pub_type

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