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Changes in apparent molar water volume and DKP solubility yield insights on the Hofmeister effect. A.Y. Payumo, R.M. Huijon, D.D. Mansfield, L.M. Belk, A.K. Bui, A.E. Knight, and D.K. Eggers, Journal of Physical Chemistry B (2011) 115, 14784-14788. DOI: 10.1021/jp206486z; PMID: 22029390 A bulk water-dependent desolvation energy model for analyzing the effects of secondary solutes on biological equilibria. D.K. Eggers, Biochemistry (2011) 50, 2004-2012. DOI: 10.1021/bi1017717; PMID: 21284393 Protein adsorption onto organically-modified silica glass leads to a different structure than sol-gel encapsulation. B. Menaa, C. Torres, M. Herrero, V. Rives, A.R.W. Gilbert, and D.K. Eggers, Biophysical Journal (2008) 95, L51-L53. DOI: 10.1529/biophysj.108.142182; PMC (free): 2553140 Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses. B. Menaa, M. Herrero, V. Rives, M. Lavrenko, and D.K. Eggers, Biomaterials (2008) 29, 2710-2718. DOI: 10.1016/j.biomaterials.2008.02.026; PMC (free): 2391299 Hydrophobic, organically-modified silica gels enhance the secondary structure of encapsulated apomyoglobin, V.A. Rocha and D.K. Eggers, Chemical Communications (2007), 1266-1268. DOI: 10.1039/B617078A; PMID: 17356778 Crowding and hydration effects on protein conformation: A study with sol-gel encapsulated proteins, D.K. Eggers and J.S. Valentine, Journal of Molecular Biology (2001) 314, 911-922. DOI: 10.1006/jmbi.2001.5166; PMID: 11734007 Molecular confinement influences protein structure and enhances thermal protein stability, D.K. Eggers and J.S. Valentine, Protein Science (2001) 10, 250-261. DOI: 10.1110/ps.36201; PMC (free): 2373941
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