Fast events in protein folding: volume and enthalpy changes and rate constants of the protonation steps leading to the compact acid intermediate of apomyoglobin
Stefania Abbruzzetti, Elisa Crema, Laura Masino, Arnaldo Vecli, Cristiano Viappiani
Dipartimento di Fisica, Università di Parma and Istituto Nazionale per la Fisica della Materia, Parma, Italia
Jeanne R. Small
Department of Chemistry and Biochemistry, Eastern Washington University,
Cheney (WA), USA
Louis J. Libertini, Enoch, W. Small
Quantum Northwest, Inc., Spokane (WA), USA
Contents
 | Abstract |
| Introduction |
| Apomyoglobin undergoes a transition from the native state to an acid intermediate at pH below 5 |
| The ultrafast pH jump methodology |
| Dependence of structural volume changes on the prepulse pH (assesment of transient identity) |
| Dependence of structural volume changes on the concentration of the protein (determination of rate constants) |
| Measurements with the several temperatures method (determination of reaction enthalpy and activation energy) |
| Conclusions |
| Acknowledgements |