Design of structurally distinct proteins using strategies inspired by evolution.
Science
; 352(6286): 687-90, 2016 May 06.
Article
en En
| MEDLINE
| ID: mdl-27151863
ABSTRACT
Natural recombination combines pieces of preexisting proteins to create new tertiary structures and functions. We describe a computational protocol, called SEWING, which is inspired by this process and builds new proteins from connected or disconnected pieces of existing structures. Helical proteins designed with SEWING contain structural features absent from other de novo designed proteins and, in some cases, remain folded at more than 100°C. High-resolution structures of the designed proteins CA01 and DA05R1 were solved by x-ray crystallography (2.2 angstrom resolution) and nuclear magnetic resonance, respectively, and there was excellent agreement with the design models. This method provides a new strategy to rapidly create large numbers of diverse and designable protein scaffolds.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Simulación por Computador
/
Ingeniería de Proteínas
/
Proteínas
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Modelos Químicos
Idioma:
En
Revista:
Science
Año:
2016
Tipo del documento:
Article
País de afiliación:
Estados Unidos