J. Phys. IV France
Volume 03, Numéro C4, Septembre 19934th International Workshop on Positron and Positronium Chemistry
|Page(s)||C4-305 - C4-310|
J. Phys. IV France 03 (1993) C4-305-C4-310
A positron annihilation lifetime study of protein hydration - evidence for a glass transitionR.B. GREGORY and K.-J. CHAI
Department of Chemistry, Kent State University, Kent, Ohio 44242, U.S.A.
Positron annihilation lifetimes have been determined for lysozyme at 298 K over the hydration range 0.007 - 0.395 h (g water / g protein) and at hydration levels of 0.15 [MATH] and 0.19 h over the temperature range 120 - 350 K. The results indicate that lysozyme undergoes a glass-like, dynamical transition with a transition temperature which decreases with increasing hydration. This behavior is similar to that found with TSDC techniques and suggests that the transitions previously observed at low hydration (0.07 - 0.2 h) at 298 K and those observed at 180 - 220 K in fully hydrated proteins are related. A second transition is observed at 160 - 170 K which may be due to protein-bound water.
© EDP Sciences 1993