Proteins: Disorder, Folding, and Crowding (Biophysical Journal)

The protein side of the central dogma of molecular biology holds that the native state of a protein is encoded by its sequence of amino acids. For more than 50 years, this principle has been largely applied to the folding of globular proteins. Both experimental and computational biophysicists have worked to determine the thermodynamic and kinetic parameters that yield underlying principles of protein folding, as well as to develop algorithms to successfully predict structure from sequence. More recently, the biophysical community has recognized that the native states of many proteins do not involve stable globular structures, but rather disordered, dynamic conformational ensembles.