Molecular dynamics of solid-state lysozyme as affected by glycerol and water: a neutron scattering study.
Glycerol has been shown to lower the heat denaturation temperature (T(m)) of dehydrated lysozyme while elevating the T(m) of hydrated lysozyme (. J. Pharm. Sci. 84:707-712). Here, we report an in situ elastic neutron scattering study of the effect of glycerol and hydration on the internal dynamics of lysozyme powder. Anharmonic motions associated with structural relaxation processes were not detected for dehydrated lysozyme in the temperature range of 40 to 450K. Dehydrated lysozyme was found to have the highest T(m) by. Upon the addition of glycerol or water, anharmonicity was recovered above a dynamic transition temperature (T(d)), which may contribute to the reduction of T(m) values for dehydrated lysozyme in the presence of glycerol. The greatest degree of anharmonicity, as well as the lowest T(d), was observed for lysozyme solvated with water. Hydrated lysozyme was also found to have the lowest T(m) by. In the regime above T(d), larger amounts of glycerol lead to a higher rate of change in anharmonic motions as a function of temperature, rendering the material more heat labile. Below T(d), where harmonic motions dominate, the addition of glycerol resulted in a lower amplitude of motions, correlating with a stabilizing effect of glycerol on the protein.
Tsai
A M
AM
Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899, USA. amos.tsai@nist.gov
Neumann
D A
DA
Bell
L N
LN
D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D002645:Chickens; D005990:Glycerol / Q000737:chemistry; D066298:In Vitro Techniques; D009113:Muramidase / Q000737:chemistry*; D009502:Neutrons; D011489:Protein Denaturation; D012542:Scattering, Radiation; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D014867:Water; D009113:Muramidase; D005990:Glycerol