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A kinetic mechanism for in vivo protein folding

Cruzeiro L.

Bio-Algorithms and Med-Systems

2014

Vol. 10, no. 3

117--127

For many decades now, the solution to the protein folding problem has been sought within the thermodynamic hypothesis of Anfinsen. Instead, the work discussed here is concerned with protein folding in vivo and assumes that the solution lies within a generalization of the kinetic, nonequilibrium mechanism first proposed by Levinthal. Accordingly, two different initial conditions, namely, a fully extended and a helical chain, are tested and pathways to the native state are generated via targeted molecular dynamics. The energetic and structural analysis indicates that a helical initial condition is to be preferred over an extended one. These results are set against the broader context of in vitro protein refolding experiments and theories and are found to be in agreement with the recent experimental observations about the influence of the ribosome on the structure of, and on the folding from, nascent chains.