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A perspective from simple exact models - UCSB College of - engineering ucsb

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The document reviews the principles of protein folding, stability, and kinetics through the lens of simple exact models. It emphasizes that the folding code is primarily encoded in the sequence of polar and nonpolar amino acids rather than local interactions. The authors argue that protein folding resembles a process of heteropolymer collapse, where secondary structures emerge as a consequence of folding rather than its cause. The study highlights the importance of nonlocal interactions and suggests that proteins are unique due to their specific sequences, which dictate their ability to fold into distinct native conformations. The findings challenge traditional views on protein structure prediction and propose new avenues for designing foldable polymers.

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