Cooperative charge fluctuations by migrating protons in globular proteins.
A review of the hydrogen bonded network on the protein surface shows the presence of a charged complex system with parallel and competitive interactions, including ionizable side-chains, migrating protons, bound water and nearby backbone peptides. This system displays cooperative effects of dynamical nature, reviewed for lysozyme as a case. By increasing the water coverage of the protein powder, the bound water cluster exhibits a percolative transition, detectable by the onset of large water-assisted displacements of migrating protons, with a parallel emergence of protein mobility and biological function. By lowering the temperature, migrating protons exhibit a glassy dielectric relaxation in the low frequency range, pointing to a frustration by competing interactions similar to that observed in spin glasses and fragile glass forming liquids. The observation of these dissipative processes implies the occurrence of spontaneous charge fluctuations. A simplified model of the protein surface, where conformational and ionizable side-chain fluctuations are averaged out, is used to discuss the statistical physics of these cooperative effects. Some biological implications of this dynamical cooperativity for enzymatic activity are briefly suggested at the end.
Careri
G
G
Dipartimento di Fisica, Universita La Sapienza, Roma, Italy.
D004798:Enzymes / Q000737:chemistry*; D006860:Hydrogen Bonding; D009113:Muramidase / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D011522:Protons; D013499:Surface Properties
D004798:Enzymes; D011506:Proteins; D011522:Protons; D009113:Muramidase