Get Time Resolved Collapse Of A Folding Protein Observed ... - Finnefrock

The energy landscape theory of protein folding is a statistical description of a protein's potential surface. It assumes that folding occurs through organizing an ensemble of structures rather than through only a few uniquely defined structural intermediates.

Under physiological conditions, a protein undergoes a spontaneous disorder ⇌ order transition called “folding.” The protein polymer is highly flexible when unfolded but adopts its unique native, three-dimensional structure when folded.

Protein folding occurs in a cellular compartment called the endoplasmic reticulum. This is a vital cellular process because proteins must be correctly folded into specific, three-dimensional shapes in order to function correctly. Unfolded or misfolded proteins contribute to the pathology of many diseases.

Anfinsen's Thermodynamic Hypothesis From his now-famous experiments on ribonuclease, Anfinsen postulated that the native structure of a protein is the thermodynamically stable structure; it depends only on the amino acid sequence and on the conditions of solution, and not on the kinetic folding route.

Time scales of milliseconds are the norm, and the fastest known protein folding reactions are complete within a few microseconds. The folding time scale of a protein depends on its size, contact order, and circuit topology.

The prevailing current view of protein folding is the thermodynamic hypothesis, under which the native folded conformation of a protein corresponds to the global minimum of Gibbs free energy G.