  Predicting the three-dimensional (3D) functional structures of proteins
remains an important computational milestone in molecular biology to be
achieved. This feat is hinged on a clear understanding of the mechanism which
proteins use to fold into their native structures. Since Levinthal's paradox,
there has been a lot of progress in understanding this mechanism. Most of the
earlier attempts were caught between assigning either hydrophobic interactions
or hydrogen bonding as the dominant folding force. However, a consensus now
seems to be emerging about hydrogen bonding being a stronger force.
Interestingly, a view from chaperone action may further throw some light on the
nature of the folding mechanism. Thus the very mechanisms which prevent protein
aggregation and misfolding, could help us have a better understanding of the
folding mechanism itself.
