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Evidence from mixed hydrate nucleation for a funnel model of crystallization

Significance Molecular crystallization, and its promotion and inhibition, is important across a broad range of fields. Previous work has asserted, although not substantiated, that crystallization and protein folding are somehow similar processes. Here, through detailed analysis of gas hydrate nucleation, we demonstrate that hydrate nucleation involves funnel-shaped potential energy landscapes, and put forth a funnel model of crystallization. This funnel model of crystallization provides a lens for exploring and understanding crystallization and potentially other ordering processes. We show that the phenomenological similarities between crystallization and protein folding result from underlying similarities between essential features of these microscopic ordering processes. This work thus provides a key connection between these two important but disparate research domains, thereby enabling knowledge advancement in both. The molecular-level details of crystallization remain unclear for many systems. Previous work has speculated on the phenomenological similarities between molecular crystallization and protein folding. Here we demonstrate that molecular crystallization can involve funnel-shaped potential energy landscapes through a detailed analysis of mixed gas hydrate nucleation, a prototypical multicomponent crystallization process. Through this, we contribute both: (i) a powerful conceptual framework for exploring and rationalizing molecular crystallization, and (ii) an explanation of phenomenological similarities between protein folding and crystallization. Such funnel-shaped potential energy landscapes may be typical of broad classes of molecular ordering processes, and can provide a new perspective for both studying and understanding these processes.