Related ArticlesHow high concentrations of proteins stabilize the amorphous state of calcium orthophosphate: a solid-state NMR study of the casein case.
Langmuir. 2017 Jan 17;:
Authors: De Sa Peixoto P, Silva JV, Laurent GP, Schmutz M, Thomas D, Bouchoux A, Gesan-Guiziou G
Abstract
Understanding how proteins stabilize Amorphous Calcium ortho-Phosphate (ACP) phases is of great importance in biology and for pharmaceutical or food applications. Until now, most of the former investigations about ACP-protein stability and equilibrium were performed in conditions where ACP colloidal nanoclusters are surrounded by low to moderate concentrations of peptides or proteins (15-30 g.L-1). As a result, the question of ACP-protein interactions in highly concentrated protein systems has clearly been overlooked, whereas it corresponds to actual industrial conditions such as drying or membrane filtration in the dairy industry for instance. In this study, the structure of an ACP phase is moni-tored in association with one model phosphorylated protein (casein) using solid state NMR (ssNMR) at two conditions of high protein concentration (300 and 400 g.L-1). At both con-centrations and at 25°C, it is found that the caseins maintain the mineral phase in an amorphous form with no detectable influence on its structure or size. Interestingly, and in both cases, a significant amount of the non-phosphorylated side chains interacts with ACP through H-bonds. The number of these interacting side-chains is found to be higher at the high-est casein concentration. At 45°C, which is a destabilizing temperature of ACP in protein-free conditions, the amorphous structure of the mineral phase is partially transformed at 300 g.L-1 while it remains almost intact at 400 g.L-1. These results thus clearly indicate that rising the concentration of proteins favor protein-ACP interactions and stabilize the ACP clusters more efficiently.
PMID: 28094949 [PubMed - as supplied by publisher]
Trimethylphosphine-AssistedSurface Fingerprinting of Metal Oxide Nanoparticle by 31P Solid-State NMR: A Zinc Oxide Case Study
Trimethylphosphine-AssistedSurface Fingerprinting of Metal Oxide Nanoparticle by 31P Solid-State NMR: A Zinc Oxide Case Study
Yung-Kang Peng, Lin Ye, Jin Qu, Li Zhang, Yingyi Fu, Ivo F. Teixeira, Ian James McPherson, Heyong He and Shik Chi Edman Tsang
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b12080/20160210/images/medium/ja-2015-120807_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b12080
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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Phosphate–WaterInterplay Tunes Amorphous CalciumCarbonate Metastability: Spontaneous Phase Separation and Crystallizationvs Stabilization Viewed by Solid State NMR
Phosphate–WaterInterplay Tunes Amorphous CalciumCarbonate Metastability: Spontaneous Phase Separation and Crystallizationvs Stabilization Viewed by Solid State NMR
Shifi Kababya, Assaf Gal, Keren Kahil, Steve Weiner, Lia Addadi and Asher Schmidt
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja511869g/20150105/images/medium/ja-2014-11869g_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja511869g
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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Solid-State NMR and FTIR Study of a Neuronal Calcium Sensor (NCS) Protein, Recoverin
Solid-State NMR and FTIR Study of a Neuronal Calcium Sensor (NCS) Protein, Recoverin
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Kim Potvin-Fournier , Audrey Picard-Lafond , Melanie Schneider , Geneviève Valois-Paillard , Thierry Lefèvre , Philippe Calvez , Line Cantin , Christian Salesse , Michèle Auger</br>
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Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials
From The DNP-NMR Blog:
Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials
Kobayashi, T., et al., Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials. Phys Chem Chem Phys, 2013. 15(15): p. 5553-62.
http://www.ncbi.nlm.nih.gov/pubmed/23459985
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Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials
From the The DNP-NMR Blog:
Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials
Kobayashi, T., et al., Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials. Phys Chem Chem Phys, 2013. 15(15): p. 5553-62.
http://www.ncbi.nlm.nih.gov/pubmed/23459985
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04-15-2013 08:52 AM
[NMR paper] How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Related Articles How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Chembiochem. 2005 Sep;6(9):1693-700
Authors: Lorch M, Faham S, Kaiser C, Weber I, Mason AJ, Bowie JU, Glaubitz C
Several studies have demonstrated that it is viable to use microcrystalline preparations of water-soluble proteins as...
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[NMR paper] A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c
A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex.
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 A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex.
Eur J Biochem. 1992 Sep 15;208(3):713-20
Authors: Tuzi S,...