4.5 Article

Frustration, function and folding

Journal

CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 48, Issue -, Pages 68-73

Publisher

CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2017.09.006

Keywords

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Funding

  1. Consejo de Investigaciones Cientificas y Tecnicas (CONICET)
  2. Agencia Nacional de Promocion Cientifica y Tecnologica [PICT2012/01647]
  3. ECOS Sud - MINCyT [A14E04]
  4. National Institute of General Medical Sciences [R01GM44557, P01-GM071862]
  5. Rice University [C-0016]

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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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