IQUIBICEN   23947
INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CIENCIAS EXACTAS Y NATURALES
Unidad Ejecutora - UE
artículos
Título:
Frustration, function and folding
Autor/es:
WOLYNES PG; FERREIRO DU; KOMIVES EA
Revista:
CURRENT OPINION IN STRUCTURAL BIOLOGY
Editorial:
CURRENT BIOLOGY LTD
Referencias:
Lugar: Londres; Año: 2018
ISSN:
0959-440X
Resumen:
Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, powerful catalysis, are examples of basic chemical activities that the great majority of polypeptides do not display, and are thought to be the outcome of the natural history of proteins. Function, a concept genuine to Biology, is at the core of evolution and often conflicts with the physical constraints. Locating the frustration between discrepant goals in a recurrent system leads to fundamental insights about the chances and necessities that shape the encoding of biological information.