The lack of a well-defined structure of Tau protein in the context of the mechanisms making functional proteins adepted to the environment

Abstract
The process of protein folding from the unfolded sequence of amino acids defining a particular protein displays a very narrow range of stability energy as measured by the ΔG° value associated with the process. The Gaussian distribution of ΔG° values obtained from a Data Base, constituted by more than five hundred data points from protein folding processes renders an average value of ΔG° = −30.9 kJ/mol. This is extremely low value, approximately equivalent to the energy involved in the formation of two hydrogen bonds, considering that a protein solution may include a vast number of hydrogen bonds and other weak interactions in water solutions. I present here two thermodynamic approaches to explain this low range of stability energy because of environmental conditions, and how many proteins, like for example Tau protein, avoiding conformational restrictions, may take advantage of its intrinsic disorder to attend a multiplicity of functions.

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