Proteins refolding

Simon I 1985 Investigation of protein refolding a special feature of native structure responsible for refolding ability J. Theor. Bioi. 113 703-10... 

In 1984, Magnuson et al. (Entry 1) investigated the influence of ethylammoni-um/water mixtures on enzyme activity and stability [29]. At low [H3NEt][N03] concentrations, an increased activity of alkaline phosphatase was found. The same ionic liquid was used by Flowers and co-workers, who found improved protein refolding after denaturation (Entry 2) [30]. 

Recently, SPE was determined to be useful in a protein refolding process. Goto, Hatton, and coworkers demonstrated that SPE was the most efficient method for solubilizing denatured ribonuclease into AOT-based w/o-MEs [59]. The w/o-ME encapsulated... 

Batas, B. and Chauduri, J.B., Considerations of sample application and elution during size-exclusion chromatography-based protein refolding, /. Chromatogr. A, 864, 229, 1999. 

First, proteins refold from the denatured state, not from the hypothetical random coil state. It is the starting point of all refolding reactions, whether in a cell or in a test tube. To understand any chemical reaction, structural features of the reactant and the product must be compared to quantify the changes that occur, for these changes define the reaction. 

Minami, Y. et al. (2000a) A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding./. Biol. Chem. 275(12), 9055-9061. 

Fig. 5. The effect of protein-protein interactions on Nephila edulis major ampullate circular dichroism spectra in solution. A change in secondary structure with increasing concentration is observed. At low concentration (minimal protein-protein interactions) silk proteins appear partially unfolded in solution. At higher concentration (higher protein-protein interactions) silk proteins refold into a helix-like structure, most likely a molten-like globule (from Dicko et al., 2004c). This final molten structure would facilitate local chain rearrangement while preserving the global structure for protein storage and transport. (Copyright 2004 American Chemical Society.)...

Dicko, C., Vollrath, F., and Kenney, J. M. (2004d). Spider silk protein refolding is controlled by changing pH. Biomacromolecules 5, 704-710. 

Proper Protein Refolding The final protein structure of the recombinant protein is often obtained by the promotion of proper refolding. When the production of recombinant proteins results in inclusion bodies, an ELISA can be used to assure that the final protein product has been properly refolded and to monitor the refolding process. To do this requires antibodies that can only recognize and bind to a particular conformation that is only present upon proper refolding. 

Tsumoto K, Umetsu M, Kumagai I, Ejima D, Philo JS, Arakawa T. Role of arginine in protein refolding, solubilization, and purification. Biotechnol Prog 2004 20(5) 1301-1308. 

R. V. Rariy and A. M. Klibanov, Protein refolding in predominantly organic media markedly enhanced by common salts, Biotechnol. Bioeng. 1999, 62, 704-710. 

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