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J Biol Chem, Vol. 274, Issue 16, 10693-10696, April 16, 1999
From the Department of Human Biological Chemistry and Genetics,
University of Texas Medical Branch, Galveston, Texas 77555-0645
A number of biologically important proteins or
protein domains identified recently are fully or partially unstructured
(unfolded). Methods that allow studies of the propensity of such
proteins to fold naturally are valuable. The traditional biophysical
approaches using alcohols to drive 
-helix formation raise serious
questions of the relevance of alcohol-induced structure to the
biologically important conformations. Recently we illustrated the
extraordinary capability of the naturally occurring solute,
trimethylamine N-oxide (TMAO), to force two unfolded
proteins to fold to native-like species with significant functional
activity. In the present work we apply this technique to recombinant
human glucocorticoid receptor fragments consisting of residues 1-500
and residues 77-262. CD and fluorescence spectroscopy showed that both
were largely disordered in aqueous solution. TMAO induced a condensed
structure in the large fragment, indicated by the substantial
enhancement in intrinsic fluorescence and blue shift of fluorescent
maxima. CD spectroscopy demonstrated that the TMAO-induced structure is
different from the -helix-rich conformation driven by
trifluoroethanol (TFE). In contrast to TFE, the conformational
transition of the 1-500 fragment induced by TMAO is cooperative, a
condition characteristic of proteins with unique structures.
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