Decoding How Proteins Fold

Abstract

The primary aims of this perspective are twofold. Firstly, to assess whether a universal principle could govern the process of protein folding. Secondly, to clarify whether the folding of a protein could be characterized by an effective trajectory, as determined by the principle of least action, while concurrently addressing the Levinthal Paradox. The effective-trajectory conjecture, which is compatible with the existence of multiple folding pathways and characterized by a single folding rate, addresses the search timescale paradox by explaining how a protein in a proper environment always reaches its native state at a consistent folding rate and in a biologically reasonable time frame (as determined by the thermodynamic hypothesis, or Anfinsen dogma). The preliminary findings support the hypothesis that the protein folding process is governed by a universal principle: that of least action. From this viewpoint, it should be regarded as a fundamental physical model that not only facilitates the identification of folding pathways and trajectories but also offers a physical framework for understanding how nature may link the optimal kinetic speed of the protein folding process with its higher thermodynamic stability.

Links & Resources

Authors

Cite This Paper