The Role of Protein 'Stability Patches' in Molecular Recognition: a Case Study of the Human Growth Hormone-Receptor Complex Abstract: Dynamic properties of protein surfaces are among the factors determining their functional properties, including their potential participation in protein-protein interactions and in binding small-molecule compounds. The presence of clusters of static residues - 'stability patches' (SPs) - is a characteristic of surfaces involved in intermolecular recognition. Comparative analyses of the surface dynamic properties of the growth hormone and of its high-affinity variant indicated that reshaping of the SPs landscape may be among the factors accountable for the improved affinity of this variant to the receptor. We hypothesized that SPs facilitate molecular recognition by moderating the conformational entropy of the unbound state, diminishing enthalpy-entropy compensation upon binding, and by augmenting the favorable entropy of desolvation. The analysis of protein surfaces emerges as a valuable tool for investigating the structural basis of the stability of protein complexes and for rationalizing experimental approaches, such as affinity.