Frustration, function and folding

Artículo

Autoría

FERREIRO, DIEGO ULISES ; Komives, Elizabeth A. ; Wolynes, Peter G.

Fecha

2018

Editorial y Lugar de Edición

Current Biology

Revista

CURRENT OPINION IN STRUCTURAL BIOLOGY, vol. 48 (pp. 68-73) Current Biology

Resumen Información suministrada por el agente en SIGEVA

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... 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.

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Palabras Clave

Protein functionProtein folding

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http://hdl.handle.net/11336/93870