Asparagine solubility

Fibrinogen (factor I, 340 kDa see Figures 51-1 and 51-4 and Tables 51-1 and 51-2) is a soluble plasma glycoprotein that consists of three nonidentical pairs of polypeptide chains (Aa,Bpy)2 covalently linked by disulfide bonds. The B(3 and y chains contain asparagine-linked complex oligosaccharides. All three... 

L-Asparagine occurs as white crystals or as a crystalline powder. It is soluble in water and practically insoluble in alcohol and in ether. Its solutions are acid to litmus. It melts at about 234°. 

In this reaction, an hydroxide ion attacks the carbonyl group of the amide to form an anionic tetrahedral intermediate followed by expulsion of the -NHR moiety. Deamidation of glutamine and asparagine residues leads to a more acidic protein derivative that may have changed solubility and functional properties. 

In some cases, mutation of surface or active site residues has been required to improve stability and solubility. Mutation of surface cysteines prevented the formation of disulfide-linked aggregates in FGFRl [54]. Mutation of highly conserved, active site residues, to create a kinase-dead mutant, was required for a number of kinases whose over-expression proved to be toxic to cells. The conserved aspartic acid in the DFG motif was mutated to an asparagine in CDK5 while the conserved lysine in PAR was mutated to an arginine [48, 51]. 

If, on the contrary, they are submitted to the action of products of the second class with non-superposable image—asparagine, quinine, strychnine, brucine, albumen, sugar, etc., bodies as)m(imetric like themselves—all is changed in an instant. The solubility is no longer the same. If combination takes place, the crystalline form, the specific weight, the quantity of water of crystallisation, the more or less easy destruction by heating, all differ as much as in the case of the most distantly related isomers. 

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