Nuclei of ordered solid phases of proteins in native conformations form within crucial precursors, which are metastable mesoscopic liquid clusters, existing both in the homogenous region of the solution phase diagram and in the region supersaturated with respect to an ordered solid phase. We show that the cluster exist due to the conformation flexibility of the protein molecules, leading to the exposure of hydrophobic surfaces and enhanced intermolecular binding.  We show that additives known to destabilize the native protein structure lead to enhanced cluster formation.  NMR characterization reveals that in solutions, in which clusters are present at concentrations allowing each protein molecule pass through a cluster within an hour, the protein conformational variability is significantly enhanced in comparison to solutions without clusters.  These results indicate that protein conformational flexibility might be the mechanism behind the metastable mesoscopic complexes and, hence, behind the clusters and new-phase nucleation. 

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