Mean-squared atomic displacements in hydrated lysozyme, native and denatured

Area of Science:

• Protein dynamics
• Biophysics
• Neutron scattering

Background:

• Hydrated proteins exhibit a dynamical transition above 200 K, marked by increased atomic displacements.
• This transition is often associated with biological function.

Purpose of the Study:

• To investigate if the dynamical transition in hydrated proteins is specific to native, biologically functional structures.
• To compare the atomic displacements in hydrated native and denatured lysozyme.

Main Methods:

• Elastic neutron scattering was employed to measure atomic displacements.
• The study focused on hydrated lysozyme in both native and denatured states.

Main Results:

• A sharp increase in mean-squared atomic displacements, characteristic of the dynamical transition, was observed in both hydrated native and denatured lysozyme.
• The transition temperature remained consistent across both protein states.

Conclusions:

• The dynamical transition in hydrated proteins is not exclusive to native, functional molecules.
• Protein denaturation does not abolish this fundamental dynamical behavior, suggesting it is a general property of hydrated protein systems.