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The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding

Published online by Cambridge University Press:  01 August 2000

SATOSHI SATO ,
COSIM J. SAYID  and
DANIEL P. RALEIGH
SATOSHI SATO
Affiliation:
Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400
COSIM J. SAYID
Affiliation:
Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400
DANIEL P. RALEIGH
Affiliation:
Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400 Graduate Program in Biophysics and Graduate Program in Molecular and Cellular Biology, State University of New York at Stony Brook, Stony Brook, New York 11794
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Abstract

Viscosities of aqueous solutions of guanidine hydrochloride (GuHCl) were measured in the presence of varying amounts of glucose. At high concentrations of glucose or GuHCl, the measured viscosities showed significant deviation from the values computed using a method proposed by Tanford (1966, J Biol Chem 241:3228–3232). This method was originally derived to allow the calculation of the effects of buffer or low concentrations of salts and other additives on the density and viscosity of aqueous solutions of urea or GuHCl. Recently it has been used to estimate the viscosity of denaturant solutions that contain high concentrations of viscogens. Our results show that the extrapolation of this approach to solutions of highly concentrated viscous co-solutes leads to significant errors. The implications for experimental studies of the viscosity dependence of conformational transitions in proteins is discussed.

Keywords

glucoseguanidine hydrochlorideprotein foldingviscosity
Type
FOR THE RECORD
Information
Protein Science , Volume 9 , Issue 8 , August 2000 , pp. 1601 - 1603
Copyright
© 2000 The Protein Society

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