Micelle protein

Keywords. Downstream processing. Reverse micelles, Protein/enzyme extraction. Modeling, Recent developments... 

Casein micelle proteins are primarily a8i-, as2-, /3-, and -caseins in approximate proportions 3 .8 3 1. asi-Casein has eight or nine phosphate groups, depending on the genetic variant. aS2-Casein is the most hydrophilic of the caseins. It has two disulfide bonds which, by severe heat treatment, can be caused to interact with those of /3-lactoglobulin. It also has 10 to 13 phosphate groups and is very sensitive to the calcium ion concentration (Kinsella 1984 Swaisgood 1982). 

Experimental results suggest that hydrophillic proteins tend to be solubilized within the water core of the reversed micelles, while lipophilic biomolecules can either stay in the interface or even partially exposed to the organic phase.45 Because of the protection offered by the reversed micelles, proteins were shown to maintain their functional properties.47 The retention of bioactivity depends strongly on the solvent system and it is usually not 100%.45... 

Chill JH, Louis JM, Miller C, Bax A. NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci. 2006 15 684-689. 

In this study we restrict our consideration by a class of ionic liquids that can be properly described based on the classical multicomponent models of charged and neutral particles. The simplest nontrivial example is a binary mixture of positive and negative particles disposed in a medium with dielectric constant e that is widely used for the description of molten salts [4-6], More complicated cases can be related to ionic solutions being neutral multicomponent systems formed by a solute of positive and negative ions immersed in a neutral solvent. This kind of systems widely varies in complexity [7], ranging from electrolyte solutions where cations and anions have a comparable size and charge, to highly asymmetric macromolecular ionic liquids in which macroions (polymers, micelles, proteins, etc) and microscopic counterions coexist. Thus, the importance of this system in many theoretical and applied fields is out of any doubt. 

A novel amine coupling method has been developed by Biacore in which an acidic protein is carried by a positively charged micelle (a cluster of oriented surfactant molecules). The micelle-protein complex carries a net positive charge at neutral pH, and is therefore attracted to the sensor surface (Fig. 14). 

Pouliquen G, Porcar I, Tribet C, Amiel C. 2002. Photoresponsive thickening in poly amphiphUe based physical gels the example of micelles, protein and cyclodextrin cross linkers. In Bohidar H, Dubin P, Osada Y, editors. ACS Advances in Chemistry. Series 833 (Polymer Gels Fundamentals and Applications). Chap 18, pp. 262 289. 

Most dairy products, including yogurts and cheeses, are based on casein micelles (protein globules 100nm in diameter) and whey proteins. Casein micelles and coagulated whey proteins must be examined by EM because LM techniques do not provide sufficient resolution. 

Diffraction techniques have been successfully applied and modified to learn about the structure of a wide variety of materials including magnetic materials, superconductors, glasses, micelles, proteins, polymers, and inorganic catalysts. Samples can be single crystal or powder, solid or liquid (although less commonly so). This chapter discusses the underlying diffraction principles, surveys common experimental and analysis techniqnes, and briefly discusses applications of diffraction for nanostractured materials. 

Imaging/Labeling Applications Amines/amino groups - amyloid-p (Ap) peptides " atherosclerotic plaque antibodies blood vessels caries in tooth enamel " cells chromosomes dendrimers glucose " " histone deacetylases liposomes nanoparticles " nucleic acids " phospholipid micelles " proteins/peptides " quantum dots " tumors " " " ... 

Photoresponsive Thickening in Poiyamphiphile-Based Physical Gels The Examples of Micelle, Protein, and Cyclodextrin Cross-Linkers... 

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