Temperature dependence of molecular interactions involved in defining stability of glutamine binding protein and its complex with L-glutamine.

ABSTRACT: The temperature dependence of dynamic parameters derived from nuclear magnetic resonance (NMR) relaxation data is related to conformational entropy of the system under study. This provides information such as macromolecules stability and thermodynamics of ligand binding. We studied the temperature dependence of NMR order parameter of glutamine binding protein (GlnBP), a periplasmic binding protein (PBP) highly specific to L-glutamine associated with its ABC transporter, with the goal of elucidating the dynamical differences between the respective ligand bound and free forms. We found that the protein-ligand interaction, which is stabilized at higher temperature, has a striking effect on the stability of the hydrophobic core of the large domain of GlnBP. Moreover, in contrast to what was fo

SUBMITTER: Pistolesi S 

PROVIDER: S-EPMC3513781 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature