Exploring Biomolecular Thermodynamics in Aqueous and Nonaqueous Environments Using Time-Resolved Photothermal Methods Book Chapter

Larsen, RW, Vetromile, CM, Maza, WA et al. (2013). Exploring Biomolecular Thermodynamics in Aqueous and Nonaqueous Environments Using Time-Resolved Photothermal Methods . 449-472. 10.1002/9781118523063.ch23

cited authors

  • Larsen, RW; Vetromile, CM; Maza, WA; Pham, K; Mikšovská, J

authors

abstract

  • This chapter explores biomolecular thermodynamics in aqueous and nonaqueous environments using time-resolved photothermal methods such as photoacoustic calorimetry (PAC). The PAC is applied to investigate fast thermodynamic events in ligand binding to heme proteins, heme protein model systems, and protein folding. The chapter talks about ligand migration in heme proteins such as myoglobin and horseradish peroxidase, and electron transfer in heme/copper oxidases in the solution environments. It also discusses CO myoglobin encapsulated in sol gels and reverse micelles (RM) in the nonaqueous environments. In addition, time-resolved optical/vibrational methods have been employed to examine the kinetics/dynamics of encapsulated heme proteins. The time-resolved photothermal methods offer a unique opportunity to access enthalpy and molar volume changes associated with photo-initiated processes on timescales ranging from tens of milliseconds down to tens of nanoseconds. © 2013 John Wiley & Sons, Inc. All rights reserved.

publication date

  • March 5, 2013

Digital Object Identifier (DOI)

International Standard Book Number (ISBN) 13

start page

  • 449

end page

  • 472