Journal
QUARTERLY REVIEWS OF BIOPHYSICS
Volume 38, Issue 3, Pages 245-288Publisher
CAMBRIDGE UNIV PRESS
DOI: 10.1017/S0033583506004185
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We review what has been learned about the protein-folding problem from experimental kinetic studies. These studies reveal patterns of both great richness and surprising simplicity. The patterns can be interpreted in terms of proteins possessing an energy landscape which is largely, but not completely, funnel-like. Issues such as speed limitations of folding, the robustness of folding, the origin of barriers and cooperativity and the ensemble nature of transition states, intermediate and traps are assessed using the results from several experimental groups highlighting energy-landscape ideas as an interpretive framework.
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