Ontology highlight
ABSTRACT:
SUBMITTER: Walsh ST
PROVIDER: S-EPMC21886 | biostudies-literature | 1999 May
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 19990501 10
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 ...[more]