During folding, proteins span a continuum of conformers starting from the denature and ending at the native state. Although often considered a statistical random coil, the denatured state can retain residual structure that mediates (re)folding. For instance, staphylococcal nuclease retains native-like topology in 8M urea, while nonnative lysozyme contains hydrophobic clusters held together by long-range interactions. By rapidly adjusting experimental conditions to favor native structure formation, relatively compact protein folding intermediates have been observed. These kinetic intermediates - coined molten globules - exhibit native-like secondary structure and fluctuating tertiary structure.
during folding proteins span a continuum of conformers starting from the denature and ending at the native state although often considered a statistical random coil the denatured state can retain residual structure that mediates (re)folding for instance staphylococcal nuclease retains native-like topology in 8m urea while nonnative lysozyme contains hydrophobic clusters held together by long-range interactions by rapidly adjusting experimental conditions to favor native structure formation relatively compact protein folding intermediates have been observed these kinetic intermediates - coined molten globules - exhibit native-like secondary structure and fluctuating tertiary structure