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Strategies for acquisition of resonance assignment spectra of highly dynamic membrane proteins: a GPCR case study |
Jul 27, 2023 - 10:14 PM - by nmrlearner
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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 T2â?? experiments indicate sample temperatures belowâ??â??â??25Â*°C facilitate higher CP enhancement and longer-lived transverse relaxation times. T1rho experiments indicate intermediate timescales are minimized below a sample temperature ofâ??â??â??20Â*°C. 2D DCP NCA experiments indicated optimal CP efficiency and resolution at a sample temperature ofâ??â??â??30Â*°C, corroborated by linewidth analysis in 3D NCACX atâ??â??â??30Â*°C compared toâ??â??â??5Â*°C. This optimal temperature is concluded to be directly related the lipid phase transition, measured to be betweenâ??â??â??20 and 15Â*°C based on rINEPT signal of all-trans and trans-gauche lipid acyl conformations. Our results have critical implications in acquisition of SSNMR membrane protein assignment spectra, as we hypothesize that different lipid compositions with... [Read More]
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