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• W2034386439 abstract "Using microcoil NMR technology, the uniformly 2H,15N-labeled integral membrane protein OmpX, and the phosphocholine derivative detergent Fos-10 (n-decylphosphocholine), we investigated solutions of mixed protein−detergent micelles to determine the influence of the detergent concentration on the NMR spectra of the protein. In a first step, we identified key parameters that influence the composition of the micelle solutions, which resulted in a new protocol for the preparation of well-defined concentrated protein solutions. This led to the observation that high-quality 2D [15N,1H]-transverse relaxation-optimized spectroscopy (TROSY) spectra of OmpX reconstituted in mixed micelles with Fos-10 were obtained only in a limited range of detergent concentrations. Outside of this range from about 90−180 mM, we observed a significant decrease of the average peak intensity. Relaxation-optimized NMR measurements of the rotational and translational diffusion coefficients of the OmpX/Fos-10 mixed micelles, Dr and Dt, respectively, then showed that the stoichiometry and the effective hydrodynamic radius of the protein-containing micelles are not significantly affected by high Fos-10 concentrations and that the deterioration of NMR spectra is due to the increased viscosity at high detergent concentrations. The paper thus provides a basis for refined guidelines on the preparation of integral membrane proteins for structural studies." @default.
• W2034386439 created "2016-06-24" @default.
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• W2034386439 date "2009-12-01" @default.
• W2034386439 modified "2023-09-30" @default.
• W2034386439 title "NMR Characterization of Membrane Protein−Detergent Micelle Solutions by Use of Microcoil Equipment" @default.
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• W2034386439 doi "https://doi.org/10.1021/ja907842u" @default.
• W2034386439 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2893019" @default.
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