Abstract

The mechanism by which a globular protein folds from the random-coil state into its unique three-dimensional native state is a subject of growing scientific and clinical importance and is a critical biophysical problem that remains to be solved. The solution to the folding problem will explain how information encoded in a DNA sequence leads to the formation of active biological molecules and will permit the design and synthesis of active, stable proteins with industrial, medical, and biotechnological uses. Using near-real-time time-resolved laser-based spectroscopic methods, we follow the refolding of a bacterial protein and report what we believe to be the first direct evidence of structural annealing in the protein core.

© 1995 Optical Society of America