Abstract
Statistical thermodynamics allows develop theoretical estimation of association entropy of molecular binding. Protein's binding studies have been helpful in the biology and pharmacology development. Using different computational techniques was calculated entropy changes on the conformational entropy in molecular binding of IgD1-3 lysozyme complex, and were took into account the effects of the solvent. Entropy changes were calculated as the difference between the entropy of the side chains involved in the binding of the complex when they participate in the link and when they are free. The theoretical results partially reproduce some experimental observations. The discrepancies can be attributed to the absence of precise data about the effects of the solvent in the complex binding.
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