Journal
ANNUAL REVIEW OF BIOPHYSICS, VOL 47
Volume 47, Issue -, Pages 223-250Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-070816-033743
Keywords
molecular recognition; lead design; protein engineering; isothermal titration calorimetry; water networks; molecular dynamics
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Funding
- Austrian Science Fund FWF [J 3771] Funding Source: Medline
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Biomolecular recognition can be stubborn; changes in the structures of associating molecules, or the environments in which they associate, often yield compensating changes in enthalpies and entropies of binding and no net change in affinities. This phenomenon-termed enthalpy/entropy (H/S) compensation-hinders efforts in biomolecular design, and its incidence-often a surprise to experimentalists-makes interactions between biomolecules difficult to predict. Although characterizing H/S compensation requires experimental care, it is unquestionably a real phenomenon that has, from an engineering perspective, useful physical origins. Studying H/S compensation can help illuminate the still-murky roles of water and dynamics in biomolecular recognition and self-assembly. This review summarizes known sources of H/S compensation (real and perceived) and lays out a conceptual framework for understanding and dissecting-and, perhaps, avoiding or exploiting-this phenomenon in biophysical systems.
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