Strategies for acquisition of resonance assignment spectra of highly dynamic membrane proteins: a GPCR case study.

ABSTRACT: In protein nuclear magnetic resonance (NMR), chemical shift assignment provides a wealth of information. However, acquisition of high-quality solid-state NMR spectra depends on protein-specific dynamics. For membrane proteins, bilayer heterogeneity further complicates this observation. Since the efficiency of cross-polarization transfer is strongly entwined with protein dynamics, optimal temperatures for spectral sensitivity and resolution will depend not only on inherent protein dynamics, but temperature-dependent phase properties of the bilayer environment. We acquired 1-, 2-, and 3D homo- and heteronuclear experiments of the chemokine receptor CCR3 in a 7:3 phosphatidylcholine:cholesterol lipid environment. 1D direct polarization, cross polarization (CP), and T₂' experiments

SUBMITTER: van Aalst EJ 

PROVIDER: S-EPMC10838152 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature