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Critical fluctuations in proteins native states
We study a large data set of protein structure ensembles of very diverse
sizes determined by nuclear magnetic resonance. By examining the
distance-dependent correlations in the displacement of residues pairs and
conducting finite size scaling analysis it was found that the correlations and
susceptibility behave as in systems near a critical point implying that, at the
native state, the motion of each amino acid residue is felt by every other
residue up to the size of the protein molecule. Furthermore certain protein's
shapes corresponding to maximum susceptibility were found to be more probable
than others. Overall the results suggest that the protein's native state is
critical, implying that despite being posed near the minimum of the energy
landscape, they still preserve their dynamic flexibility
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