Random matrix approach to collective behavior and bulk universality in protein dynamics.
Covariance matrices of amino acid displacements, commonly used to characterize the large-scale movements of proteins, are investigated through the prism of random matrix theory. Bulk universality is detected in the local spacing statistics of noise-dressed eigenmodes, which is well described by a Brody distribution with parameter beta approximately = 0.8. This finding, supported by other consistent indicators, implies a novel quantitative criterion to single out the collective degrees of freedom of the protein from the majority of high-energy, localized vibrations.
Potestio
Raffaello
R
Scuola Internazionale Superiore di Studi Avanzati, Via Beirut 2/4-34151 Trieste, Italy.
Caccioli
Fabio
F
Vivo
Pierpaolo
P
D009068:Movement; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D014732:Vibration
D011506:Proteins