In its native state, the treasure trove of nutrients and biochemical machinery known as egg white is a slimy, translucent soup of proteins. Heat it atop a stove, however, and the proteins unfold, coagulate, and collectively morph into an opaque white solid. The unraveled proteins are said to have denatured. The enzymes among them, although well-suited for a cheese omelet, are in no shape to usher along biochemical reactions.

The proteins would have suffered a similar fate had the egg white been whipped into a foamy meringue or soaked in lime juice. Indeed, the precise biological work of folding a protein can be undone by any number of environmental stresses, including heat, acidity, and mechanical strain. Proteins, like all molecules, tend to adopt the shape that minimizes their free energy. In some circumstances, a compactly folded state makes thermodynamic sense; in others, it doesn’t.

To characterize the influence of environment...

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