We present here a study of the dynamics of two monomeric proteins, trypsin and lysozyme, by means of elastic and quasielastic neutron scattering under medium-to-high pressure conditions (1-1200 bar). The internal motions as probed from the average proton dynamics in the 100 ps timescale have a confined diffusive nature. On increasing the pressure up to 1200 bar the confinement volume is almost unaffected, while the fraction of protons involved is slightly decreased.
Filabozzi, A., Di Bari, M., Deriu, A., DI VENERE, A., Andreani, C., Rosato, N. (2005). Pressure dependence of protein dynamics investigated using elastic and quasielastic neutron scattering. In Journal of Physics Condensed Matter (pp.S3101-S3109). BRISTOL : IOP PUBLISHING LTD [10.1088/0953-8984/17/40/013].
Pressure dependence of protein dynamics investigated using elastic and quasielastic neutron scattering
FILABOZZI, ALESSANDRA;DI VENERE, ALMERINDA;ANDREANI, CARLA;ROSATO, NICOLA
2005-01-01
Abstract
We present here a study of the dynamics of two monomeric proteins, trypsin and lysozyme, by means of elastic and quasielastic neutron scattering under medium-to-high pressure conditions (1-1200 bar). The internal motions as probed from the average proton dynamics in the 100 ps timescale have a confined diffusive nature. On increasing the pressure up to 1200 bar the confinement volume is almost unaffected, while the fraction of protons involved is slightly decreased.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
