High-resolution protein design with backbone freedom.
Science
; 282(5393): 1462-7, 1998 Nov 20.
Article
em En
| MEDLINE
| ID: mdl-9822371
ABSTRACT
Recent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form alpha-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Conformação Proteica
/
Engenharia de Proteínas
/
Proteínas
/
Dobramento de Proteína
Idioma:
En
Revista:
Science
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Estados Unidos