How do proteins find their native shape? This review explores the energy landscape theory of protein folding, offering a statistical perspective on a protein’s potential surface. The theory posits that proteins fold by organizing an ensemble of structures rather than through specific intermediates, suggesting that a realistic protein model is a minimally frustrated heteropolymer with a rugged funnel-like energy landscape biased toward the native state. Analytical tools from statistical mechanics, polymer physics, and phase transitions are used to develop this description. The theory contrasts phenomena in homopolymers, random heteropolymers, and protein-like heteropolymers, linking these concepts to results from minimalist computer simulations. It concludes with a discussion of how the theory aids in interpreting results from fast folding experiments and predicting protein structures.
Published in the Annual Review of Physical Chemistry, this article aligns with the journal’s focus on theoretical and experimental aspects of physical chemistry. The review of the energy landscape theory of protein folding contributes to understanding the physical principles governing protein behavior, a topic relevant to the journal’s scope.
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