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Lim, W.K., Rosgenc, J. and Englandera, S.W. (2009) Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group. Proceedings of the National Academy of Sciences USA, 106, 2595-2600. doi:10.1073/pnas.0812588106

has been cited by the following article:

• TITLE: Microwave based reversible unfolding and refolding of alcohol oxidase protein probed by fluorescence and circular dichroism spectroscopy

  AUTHORS: Soma Sekhar R. Chinnadayyala, M. Santhosh, Pranab Goswami

  KEYWORDS: Microwave; Alcohol Oxidase; Protein Unfolding; Protein Refolding; Pichia Pastoris; Protein structure

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.3 No.4, November 29, 2012

  ABSTRACT: The reversible effect of microwave mediated denaturation of protein at low exposure time of 10 s has been demonstrated for the first time. The effect of microwave (2.45 GHz and 900 W) was confirmed in a homo-octameric alcohol oxidase in aqueous solution of pH 7.5. The unfolding events did not transverse through any intermediate states and no subunits of the protein were detached during the process. The refolding of the protein achieved at 4℃ for 24 h had regenerated the native enzyme. This reversible refolding approach excludes any chemical reagent and therefore established as simple technique for protein unfolding-folding studies.