Send to

Choose Destination
Curr Opin Struct Biol. 2018 Feb;48:68-73. doi: 10.1016/ Epub 2017 Nov 5.

Frustration, function and folding.

Author information

Protein Physiology Lab, FCEyN-Universidad de Buenos Aires, IQUIBICEN/CONICET, Intendente Güiraldes 2160, Ciudad Universitaria, C1428EGA Buenos Aires, Argentina.
Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92092-0378, USA.
Center for Theoretical Biological Physics, Rice University, Houston, TX, USA; Department of Chemistry, Rice University, Houston, TX, USA; Department of Physics, Rice University, Houston, TX, USA; Department of Biosciences, Rice University, Houston, TX, USA.


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.

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center