Long-range correlation in protein dynamics: Confirmation by structural data and normal mode analysis
Fig 1
The critical dynamics of proteins are robustly encoded in the native structure.
(A) An illustration of the elastic network model (rC = 9Å) of the protein CI2 (PDB code: 2CI2). The beads denote the residues, and the bonds denote the elastic springs in the model. (B) The correlation functions ϕ(r) for proteins at different sizes predicted by GNM with cutoff distance rC = 9Å. (C) Correlation functions scaled by the radius of gyration of the proteins Rg. (D) For proteins of similar sizes (19.5Å ≤ Rg < 20.5Å), with different cutoff distances rC, the correlation functions ϕ(r) predicted by GNM. (E) With different cutoff distances, for proteins of different sizes, the correlation length ξ is always proportional to the size of the protein Rg. (F) The susceptibility χ vs. chain length N shows the power-law relation: χ ∼ Nαγ/ν, and the scaling coefficient αγ/ν ≈ 1 can be kept with different rC (inset).