Abstract
The successful confinement of proteins in solid state materials allows for a multitude of applications in the study of protein dynamics, as well as, advances in biotechnologies. The importance of bulk solvent and restricted space on the conformational dynamics of proteins can be identified by encapsulating the biomolecules (peptides, proteins, enzymezes, etc) in environments where both can be regulated. In addition, the affect of encapsulation on ligand binding and preservation of reactivity once encapsulated are of equal importance. With the use of Photoacoustic calorimetry (PAC) and Photothermal beam deflection (PBD) methods along with picosecond-millisecond transient absorption and fluorescence techniques we are investigating enthalpy, molar volume changes, and kinetics associated with with CO dissociation and rebinding to horse heart myoglobin encapsulated in sol-gels. Preliminary PAC data suggest that the dissociation of CO from HHMb results in four kinetic phases: <7ns, ∼125ns, ∼260ns, and ∼600ns. We will discuss the differences in molar volume and enthalpy changes associated with the conformational dynamics of these events in sol-gels relative to native protein in aqueous solution.
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