Associate Professor
Biochemistry

DH 604
(408) 924-4960
daryl.eggers@sjsu.edu

Eggers Group Page

Education

B.S., Chemical Engineering, Rose-Hulman Inst. Technol., 1981
M.S., Chemical Engineering, Univ. California, Berkeley, 1987
Ph.D., Pharmacology, Univ. California, San Francisco, 1997
Postdoctoral Fellow, Univ. California, Los Angeles, 1997-02

Courses Taught

Biochemistry
Biochemistry Lab

Research Interests

• Protein folding, especially the effects of molecular crowding and molecular confinement
• Hydration effects on biological phenomena, including protein folding & aggregation
• Sol-gel glass applications and biosilica formation

Selected Publications

• Calabretta, P.J., Chancellor, M.C., Torres, C., Abel, Jr., G.R., Niehaus, C., Birtwhistle, N.J., Khouderchah, N.M., Zemede, G.H., and D.K. Eggers: Silica as a matrix for encapsulating proteins: Surface effects on protein structure assessed by circular dichroism spectroscopy. J. Funct. Biomater. 3:514-527 (2012). 
• Payumo, A.Y., Huijon, R.M., Mansfield, D.D., Belk, L.M., Bui, A.K., Knight, A.E., and D.K. Eggers: Changes in apparent molar water volume and DKP solubility yield insights on the Hofmeister effect. J. Phys. Chem. B 115:14784-14788 (2011). 
• Eggers, D.K.: A bulk water-dependent desolvation energy model for analyzing the effects of secondary solutes on biological equilibria. Biochemistry 50:2004-2012 (2011). 
• Menaa, B., Torres, C., Herrero, M., Rives, V., Gilbert, A.R.W., and D.K. Eggers: Protein adsorption onto organically-modified silica glass leads to a different structure than sol-gel encapsulation. Biophysical J. 95:L51-L53 (2008). 
• Menaa, B., Herrero, M., Rives, V., Lavrenko, M., and D.K. Eggers: Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses. Biomaterials 29:2710-2718 (2008). 
• Rocha, V.A., and D.K. Eggers: Hydrophobic, organically-modified silica gels enhance the structure of encapsulated apomyoglobin. ChemComm, 1266-1268 (2007). 
• Rodriguez, J.A., B.F. Shaw, A. Durazo, S.H. Sohn, P. Doucette, A.M. Nersissian, K.F. Faull, D.K. Eggers, A. Tiwari, L.J. Hayward, J.S. Valentine: Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. Proc. Nat. Acad. Sci. 102:10516-21(2005). 
• Rodriguez, J.A., J.S. Valentine, D.K. Eggers, J.A. Roe, A. Tiwari, R.H. Brown, L.J. Hayward: Familial ALS-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase. J. Biol. Chem. 277:15932-37 (2002). 
• Eggers, D.K., and J.S. Valentine: Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins. J. Mol. Biol. 314:911-922 (2001). 
• Eggers, D.K., and J.S. Valentine: Molecular confinement influences protein structure and enhances thermal protein stability. Protein Science 10:250-261 (2001). 
• Eggers, D.K., W.J. Welch, and W.J. Hansen: Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol. Biol. Cell 8:1559-1573 (1997).
• Eggers, D.K., Blanch, H.W. and J.M. Prausnitz: Extractive catalysis: Solvent effects on equilibria of enzymatic reactions in two-phase systems. Enzyme Microb. Technol. 11:84-89 (1989).