Abstract
A mixture of dihexanoyl phosphatidylcholine and dimyristoylphosphatidylcholine in water forms disc-shaped particles, often referred toas bicelles [Sanders and Schwonek (1992) Biochemistry, 31, 8898–8905].These adopt an ordered, liquid crystalline phase, which can be maintained atvery low concentrations of the bicelles (down to 3% w/v). At thisconcentration the spacing between individual bicelles, on average, exceeds300 Å. The bicelles are shown to have a negligible effect on therotational diffusion of ubiquitin as judged by the 15NT1ρ values of the backbone amides relative to those inisotropic aqueous solution. The protein exhibits a residual degree ofalignment which is proportional to the bicelle concentration, andapproximately collinear with ubiquitin's rotational diffusion tensor. Thedegree of alignment obtained offers unique opportunities for studying theprotein's structure and dynamics.
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Bax, A., Tjandra, N. High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium. J Biomol NMR 10, 289–292 (1997). https://doi.org/10.1023/A:1018308717741
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DOI: https://doi.org/10.1023/A:1018308717741