For over 120 years it has been appreciated that certain salts (kosmotropes) cause the precipitation of proteins, whilst others (chaotropes) increase their solubility. The cause of this, “Hofmeister effect” is still unclear; especially with the original concept that kosmotropic anions “make” water structure and chaotropes “break” it being countered by recent studies suggesting otherwise. Here, we present the first direct evidence that chaotropic anions have an affinity for hydrophobic concavity, and that it is competition between a convex hydrophobe and the anion for a binding site that leads to the apparent weakening of the hydrophobic effect by chaotropes. In combination, these results suggest that chaotropes primarily induce protein solubilization by direct binding to concavity in the molten globule state of a protein.
A combination of hydrophobic forces and guest templation drive the assembly of cavitands into molecular capsules. Remarkably, anthracene that dimerizes with unit efficiency in solution does not dimerize within the capsule despite forming 2:2 complex. The capsule allows an unprecedented examination of the anthracene excimer.
A combination of hydrophobic forces and guest templation drive the assembly of cavitands into molecular capsules. Encapsulated guests such as dibenzyl ketones reside in an essentially dry environment, and upon irradiation, undergo rearrangement processes that are templated by the shape of the 1 nm x 2 nm cavity.
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