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| - Dissecting the Vibrational Entropy Change on Protein/Ligand Binding: Burial of a WaterMolecule in Bovine Pancreatic Trypsin Inhibitor
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| - Using normal-mode analysis, the vibrational entropy change on the burial of a crystallographically well-ordered water molecule in bovine pancreatic trypsin inhibitor (BPTI) is dissected. The vibrational entropycontent of the complex is 13.4 cal mol-1 K-1 higher than that of the unbound protein. A detailed analysis isperformed of how the translational and rotational degrees of freedom of the isolated water molecule aretransformed into vibrational modes in the complex. This process is shown to be well described by a modelof the complex in which the water molecule librates in a rigid protein cage. These librational modes contribute9.4 cal mol-1 K-1 to the entropy change. The remaining 4 cal mol-1 K-1 arises from increased protein flexibilitydue to softening of the delocalized modes, mostly in the frequency range below 50 cm-1. The dominantlibrational entropy effect suggests a method by which an estimation of the vibrational contribution to ligandbinding can be efficiently computed.
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