A fluid material with high protein content (120–310 mg mL-1) was formed through the ordered self-assembly of native proteins segregated from water. This material is instantly prepared by the simple mixing of a protein solution with anionic and cationic surfactants. By changing the ratio of the surfactants based on the electrostatic characteristics of the target protein, we observed that the surfactants could function as a versatile molecular glue for protein assembly. Moreover, these protein assemblies could be disassembled back into an aqueous solution depending on the salt conditions. Owing to the water-retaining properties of the hydrophilic part of surfactants, the proteins in this material are in a water-rich environment, which maintains their native structure and function. The inclusion of water also provides functional extensibility to this material, as demonstrated by the preparation of an enzymatically active gel. We anticipate that the unique features of this material will permit the use of proteins not only in solution but also as elements of integrated functionalized materials.Fluid protein–surfactant complex: A water-rich but water-segregated fluid material containing densely packed native proteins is instantly formed by simple mixing of a protein solution with a solution containing specific amounts of both anionic and cationic surfactants.
Dissolution Dynamic Nuclear Polarization capability study with fluid path
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Dissolution Dynamic Nuclear Polarization capability study with fluid path
p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica}
Malinowski, R.M., et al., Dissolution Dynamic Nuclear Polarization capability study with fluid path. J Magn Reson, 2016. 272: p. 141-146.
https://www.ncbi.nlm.nih.gov/pubmed/27693965
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Dissolution Dynamic Nuclear Polarization capability study with fluid path
From The DNP-NMR Blog:
Dissolution Dynamic Nuclear Polarization capability study with fluid path
p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica}
Malinowski, R.M., et al., Dissolution Dynamic Nuclear Polarization capability study with fluid path. J Magn Reson, 2016. 272: p. 141-146.
https://www.ncbi.nlm.nih.gov/pubmed/27693965
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11-19-2016 08:35 PM
Solid state NMR of salivary calculi: Proline-rich salivary proteins, citrate, polysaccharides, lipids, and organic–mineral interactions
Solid state NMR of salivary calculi: Proline-rich salivary proteins, citrate, polysaccharides, lipids, and organic–mineral interactions
Publication date: Available online 3 January 2016
Source:Comptes Rendus Chimie</br>
Author(s): Yang Li, David G. Reid, Dominique Bazin, Michel Daudon, Melinda J. Duer</br>
Solid state NMR (ssNMR) can characterize mineral (31P) and organic (13C) components of human salivary stones (n*=*8). All show apatitic 31P spectra. 13C ssNMR indicates more protein, of more consistent composition, than apatitic uroliths, with prominent...
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University of Lille: Postdoc: Characterization of the condensed and gaseous phases of flame retarted materials upon bu...
University of Lille: Postdoc: Characterization of the condensed and gaseous phases of flame retarted materials upon bu...
University of Lille:The objectives of this postdoc deals with the development of methods to characterize degraded materials by physico-chemical analytical methods (methods ex-situ). It will particularly focus on solid state NMR methodology and analytical methods (e.g. FTIRFrance
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Authors: Arnold A, Paris M, Auger M
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Authors: Bloom M
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Study of the interaction between salivary proline-rich proteins and a polyphenol by 1H-NMR spectroscopy.
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Study of the interaction between salivary proline-rich proteins and a polyphenol by 1H-NMR spectroscopy.
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