Probing excited states and activation energy for the integral membrane protein phospholamban by NMR CPMG relaxation dispersion experiments.

ABSTRACT: Phospholamban (PLN) is a dynamic single-pass membrane protein that inhibits the flow of Ca(2+) ions into the sarcoplasmic reticulum (SR) of heart muscle by directly binding to and inhibiting the SR Ca(2+)ATPase (SERCA). The PLN monomer is the functionally active form that exists in equilibrium between ordered (T state) and disordered (R state) states. While the T state has been fully characterized using a hybrid solution/solid-state NMR approach, the R state structure has not been fully portrayed. It has, however, been detected by both NMR and EPR experiments in detergent micelles and lipid bilayers. In this work, we quantitatively probed the mus to ms dynamics of the PLN excited states by observing the T state in DPC micelles using CPMG relaxation dispersion NMR spectroscopy under functio

SUBMITTER: Traaseth NJ 

PROVIDER: S-EPMC3328355 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature