Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection

Energy landscape Sequence space Molecular evolution Folding (DSP implementation) Sequence (biology) Protein evolution Energetics
DOI: 10.1073/pnas.1413575111 Publication Date: 2014-08-12T06:59:19Z
ABSTRACT
Significance Natural protein sequences, being the result of random mutation coupled with natural selection, have remarkable properties that are not typical unselected including ability to robustly fold an organized structure is needed function. We estimate selection temperature, effective temperature at which sequences were selected by evolution, for eight families and compare these values experimental data folding temperatures proteins in each family. The measures importance maintaining stability structural specificity folded state on evolutionary process. For all families, below physiological indicating integrity important constraint evolution.
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