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Published online before print September 30, 2005, 10.1110/ps.051535405
Protein Science (2005), 14:2919-2921. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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FOR THE RECORD

Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids

Ronald W. Peterson, Maxim S. Pometun, Zhengshuang Shi and A. Joshua Wand

Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USA

(RECEIVED April 22, 2005; FINAL REVISION July 22, 2005; ACCEPTED July 22, 2005)

NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids is emerging as a tool for biophysical studies of proteins in atomic detail in a variety of otherwise inaccessible contexts. The central element of the approach is the encapsulation of the protein of interest within the aqueous core of a reverse micelle with high structural fidelity. The process of encapsulation is highly dependent upon the nature of the surfactant(s) employed. Here we describe novel mixtures of surfactants that are capable of successfully encapsulating a range of types of proteins under a variety of conditions.

Keywords: reverse micelle; mixed surfactant systems; NMR spectroscopy; protein encapsulation

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051535405.

Reprint requests to: A. Joshua Wand, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104-6059, USA; e-mail: wand{at}mail.med.upenn.edu; fax: (215) 573-7290.


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