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How Nothing Boosts Affinity: Hydrophobic Ligand Binding to the Virtually Vacated S1′ Pocket of Thermolysin

The positions of bound xenon and krypton in the crystal structure can be unambiguously identified in the electron density due to their anomalous scattering properties. Both types of noble gases populate the same position in the S1′ cavity.

Krimmer S G et al., J. Am. Chem. Soc., 2017, 139 (30), pp 10419–10431
 The hydration state of deep, well-accessible hydrophobic pocket of the metalloprotease thermolysin has been investigated using high-resolution crystallography and isothermal titration calorimetry to understand solvent effects in protein−ligand interactions, a key topic in drug design. The enzyme accessibility could be proved by accommodating noble gas atoms into the pocket in the crystalline state. The noble gases xenon and krypton are known to preferentially bind to desolvated, hydrophobic protein cavities through weak van der Waals interactions. These atoms can, therefore, be used as experimental probes to detect such cavities.

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How Nothing Boosts Affinity: Hydrophobic Ligand Binding to the Virtually Vacated S1′ Pocket of Thermolysin.

Krimmer S G, Cramer J, Schiebel J, Heine A, Klebe G, J. Am. Chem. Soc., 2017, 139 (30), pp 10419–10431 DOI: 10.1021/jacs.7b05028



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