| Literature DB >> 16199658 |
Ronald W Peterson1, Maxim S Pometun, Zhengshuang Shi, A Joshua Wand.
Abstract
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.Mesh:
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Year: 2005 PMID: 16199658 PMCID: PMC2253227 DOI: 10.1110/ps.051535405
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725