FASEB J. Thermo Fisher Scientific
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The FASEB Journal, Vol 10, 164-170, Copyright © 1996 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

Spectroscopic and volumetric investigation of cytochrome c unfolding at alkaline pH: characterization of the base-induced unfolded state at 25 degrees C

TV Chalikian, VS Gindikin and KJ Breslauer
Department of Chemistry, Rutgers, State University of New Jersey, Piscataway 08855, USA.

We have measured at 25 degrees C the relative specific sound velocity increment, [u], and the partial specific volume, v degrees, of cytochrome c as a function of pH. Our data reveal that the base-induced native to unfolded transition of the protein is accompanied by a volume decrease of 0.014 cm3 g-1 and a compressibility decrease of 3.8 x 10(- 6) cm3 g-1 bar-1. These results allow us to conclude that, relative to a fully unfolded conformation, the base-denatured state of cytochrome c has only 70 to 80% of its surface area exposed to the solvent. Recently, we reported a similar result for the acid-denatured state of cytochrome c. Thus, insofar as solvent exposure is concerned, both the base- and the acid-induced unfolded states of cytochrome c retain some order, with 20 to 30% of their surface areas remaining solvent- inaccessible. We discuss the implications of this result in terms of defining potential intermediate states in protein folding pathways.


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M. Ye, Q.-L. Zhang, H. Li, Y.-X. Weng, W.-C. Wang, and X.-G. Qiu
Infrared Spectroscopic Discrimination between the Loop and {alpha}-Helices and Determination of the Loop Diffusion Kinetics by Temperature-Jump Time-Resolved Infrared Spectroscopy for Cytochrome c
Biophys. J., October 15, 2007; 93(8): 2756 - 2766.
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Copyright © 1996 by The Federation of American Societies for Experimental Biology.