Abstract
The ability of protein molecules to fold into their highly structured
functional states is one of the most remarkable evolutionary
achievements of biology. In recent years, our understanding of the way
in which this complex self-assembly process takes place has increased
dramatically. Much of the reason for this advance has been the
development of energy surfaces (landscapes), which allow the folding
reaction to be described and visualized in a meaningful manner.
Analysis of these surfaces, derived from the constructive interplay
between theory and experiment, has led to the development of a unified
mechanism for folding and a recognition of the underlying factors that
control the rates and products of the folding process.
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