Jörg Rösgen, B. Montgomery Pettitt, David Wayne Bolen

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Protein Folding, Stability, and Solvation Structure in Osmolyte Solutions Jörg Rösgen, B. Montgomery Pettitt, David Wayne Bolen Biophysical Journal Volume 89, Issue 5, Pages 2988-2997 (November 2005) DOI: 10.1529/biophysj.105.067330 Copyright © 2005 The Biophysical Society Terms and Conditions

Figure 1 Volume fraction dependence of the radial distribution functions gαβ and Kirkwood G factors in an example liquid system with Lennard-Jones potential. Functions shown for packing fractions 15, 25, 35, and 45%. (1) At distances closer than the sum of the two radii (contact distance), steric exclusion is operative. (2) At intermediate distances, there are strongly concentration-dependent solvation features, most notably the first solvation shell just outside the region of steric exclusion. (3) At large distances there is no correlation between particles and the pair correlation function approaches unity. The inset shows the Kirkwood-Buff integrals (Eq. 1) as a function of the packing fraction. Note the slope and sign changes with respect to packing fraction. Biophysical Journal 2005 89, 2988-2997DOI: (10.1529/biophysj.105.067330) Copyright © 2005 The Biophysical Society Terms and Conditions

Figure 2 Change in solvation preference ΔND(GPW−GPO): dependence on osmolyte concentration (normalized to solvation preference at 0M). The curves were calculated from Eq. 8 using osmolyte activity coefficient data (22) assuming a constant m-value. In the case of the denaturing osmolyte urea the solvation preference deviates plus or minus a few percent. In the case of the protecting osmolytes (except glycine), it changes two- to fourfold. The curves are labeled at the right end: u=urea. Polyols are: go=glycerol, e=erythritol, ma=mannitol, so=sorbitol. Amino acids are: g=glycine, a=alanine, p=proline, sa=sarcosine, gb=glycine betaine. Saccharides are: x=xylose, f=fucose, gl=glucose, ga=galactose, rh=rhamnose, mo=mannose, mt=maltose, su=sucrose, ra=raffinose. Biophysical Journal 2005 89, 2988-2997DOI: (10.1529/biophysj.105.067330) Copyright © 2005 The Biophysical Society Terms and Conditions