The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The search session has expired. Please query the service again.
The paper reports a study on the kinetics of the transition between acid and alkaline Aplysia myoglobin. The results, obtained with the temperature-jump method, show that the observed relaxation effect corresponds to a perturbation of the equilibrium between the protonated and deprotonated forms of the protein. The pH dependence of the data and their analysis suggest that the process involves a proton-linked conformational change of the protein, in agreement with independent experiments. The comparison...
Download Results (CSV)