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Polymers, Volume 12, Issue 2 (February 2020) – 238 articles
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Cover Story (view full-size image) The thermophoretic response of a protein is sensitive to ligand binding, provides access to [...] Read more. The thermophoretic response of a protein is sensitive to ligand binding, provides access to equilibrium binding constants, and is remarkably sensitive to changes in the hydration layer. Systematic thermophoretic measurements of the protein streptavidin and the streptavidin-biotin complex using thermal diffusion forced Rayleigh scattering showed that free streptavidin is more thermophobic and slightly more hydrophilic compared with the streptavidin-biotin complex. The ligand-bound complex most likely forms fewer hydrogen bonds with surrounding water molecules, leading to an entropy increase of the released water molecules, which partially compensates for the conformational entropy loss of streptavidin upon binding biotin. View this paper.