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. Author manuscript; available in PMC: 2010 Jun 2.
Published in final edited form as: Biochemistry. 2009 Jun 2;48(21):4577–4586. doi: 10.1021/bi900273j

Figure 2.

Figure 2

The relative number of different potential reaction events, W(r)=4πr2Prx(r), among solute molecules that may be encountered by hydroxyl radicals as a function of distance (Å) from a point source, in 10% v/v glycerol (solid curve at lower left corner), 1% v/v glycerol (dashed curve), and 0.1% v/v glycerol (dot-dashed curve). The vertical scale is arbitrary. Glycerol is considered part of the solvent. Also shown, for a 5 μM protein solution, are vertical lines marking the average protein-protein nearest-neighbor distance nnd = 384Å, and distances one standard deviation (139Å) closer, nnd – σ, and two standard deviations closer, nnd – 2σ. For a 5 μM solution containing 10% v/v glycerol, hydroxyl radical encounters are effectively confined to the protein complex from which the radical originates.