Effect of the environment on the protein dynamical transition: a neutron scattering study.
We performed an elastic neutron scattering investigation of the molecular dynamics of lysozyme solvated in glycerol, at different water contents h (grams of water/grams of lysozyme). The marked non-Gaussian behavior of the elastic intensity was studied in a wide experimental momentum transfer range, as a function of the temperature. The internal dynamics is well described in terms of the double-well jump model. At low temperature, the protein total mean square displacements exhibit an almost linear harmonic trend irrespective of the hydration level, whereas at the temperature T(d) a clear changeover toward an anharmonic regime marks a protein dynamical transition. The decrease of T(d) from approximately 238 K to approximately 195 K as a function of h is reminiscent of that found in the glass transition temperature of aqueous solutions of glycerol, thus suggesting that the protein internal dynamics as a whole is slave to the environment properties. Both T(d) and the total mean square displacements indicate that the protein flexibility strongly rises between 0.1 and 0.2h. This hydration-dependent dynamical activation, which is similar to that of hydrated lysozyme powders, is related to the specific interplay of the protein with the surrounding water and glycerol molecules.
Istituto Nazionale per la Fisica della Materia, Dipartimento di Fisica dell'Università di Perugia, Perugia 06121, Italy. alessandro.paciaroni@fisica.unipg.it
Alessandro
A
Paciaroni
Stefania
S
Cinelli
Giuseppe
G
Onori
D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D002645:Chickens; D005990:Glycerol / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry; D009502:Neutrons; D011506:Proteins / Q000737:chemistry*; D012542:Scattering, Radiation; D013696:Temperature; D014867:Water / Q000737:chemistry
D011506:Proteins; D014867:Water; D009113:Muramidase; D005990:Glycerol