SEARCH

SEARCH BY CITATION

References

  • Acampora, G. and Hermans, J. 1967. Reversible denaturation of sperm whale myoglobin. I. Dependence on temperature, pH, and composition. J. Am. Chem. Soc. 89: 15431552.
  • Badjic, J. and Kostic, N.M. 1999. Effects of encapsulation in sol-gel silica glass on esterase activity, conformational stability, and unfolding of bovine carbonic anhydrase II. Chem. Mater. 11: 36713679.
  • Baldwin, R.L. 1996. How Hofmeister ion interactions affect protein stability. Biophys. J. 71: 20562063.
  • Braun, S., Rappoport, S., Zusman, R., Avnir, D., and Ottolenghi, M. 1990. Biochemically active sol-gel glasses: The trapping of enzymes. Materials Lett. 10: 15.
  • Chen, W., Helenius, J., Braakman, I., and Helenius, A. 1995. Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl. Acad. Sci. 92: 62296233.
  • Collins, K.D. 1997. Charge density-dependent strength of hydration and biological structure. Biophys. J. 72: 6576.
  • Collins, K.D. and Washabaugh, M.W. 1985. The Hofmeister effect and the behavior of water at interfaces. Q. Rev. Biophys. 18: 323422.
  • Dave, B.C., Dunn, B., Valentine, J.S., and Zink, J.I. 1994. Sol-gel encapsulation methods for biosensors. Anal. Chem. 66: 1120A1127A.
  • Du, Q., Freysz, E., and Shen, Y.R. 1994. Vibrational spectra of water molecules at quartz/water interfaces. Phys. Rev. Lett. 72: 238241.
  • Edmiston, P.L., Wambolt, C.L., Smith, M.K., and Saavedra, S.S. 1994. Spectroscopic characterization of albumin and myoglobin entrapped in bulk sol-gel glasses. J. Colloid Interface Sci. 163: 395406.
  • Ellerby, L.M., Nishida, C.R., Nishida, F., Yamanaka, S.A., Dunn, B., Valentine, J.S., and Zink, J.I. 1992. Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method. Science 255: 11131115.
  • Ellis, R.J. 1997. Molecular chaperones: Avoiding the crowd. Curr. Biol. 7: R531R533.
  • Ewbank, J.J. and Creighton, T.E. 1993. Structural characterization of the disulfide folding intermediates of bovine α-lactalbumin. Biochemistry 32: 36943707.
  • Gast, K., Zirwer, D., Muller-Frohne, M., and Damaschun, G. 1999. Trifluoroethanol-induced conformational transitions of proteins: Insights gained from the differences between α-lactalbumin and ribonuclease A. Protein Sci. 8: 625634.
  • Goto, Y. and Fink, A.L. 1990. Phase diagram for acidic conformational states of apomyoglobin. J. Mol. Biol. 214: 803805.
  • Gottfried, D.S., Kagan, A., Hoffman, B.M., and Friedman, J.M. 1999. Impeded rotation of a protein in a sol-gel matrix. J. Phys. Chem. B 103: 28032807.
  • Hapner, K.D., Bradshaw, R.A., Hartzell, C.R., and Gurd, F.R.N. 1968. Comparison of myoglobins from harbor seal, porpoise, and sperm whale. J. Biol. Chem. 243: 683689.
  • Hardesty, B., Tsalkova, T., and Kramer, G. 1999. Co-translational folding. Curr. Op. Struct. Biol. 9: 111114.
  • Hirota, N., Mizuno, K., and Goto, Y. 1997. Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci. 6: 416421.
  • Ishida, T. and Makino, T. 1999. Microwave dielectric relaxation of bound water to silica, alumina, and silica-alumina gel suspensions. J. Colloid Interface Sci. 212: 144151.
  • Kondo, A. and Mihara, J. 1996. Comparison of adsorption and conformation of hemoglobin and myoglobin on various inorganic ultrafine particles. J. Colloid Interface Sci. 177: 214221.
  • Kundu, B. and Guptasarma, P. 1999. Hydrophobic dye inhibits aggregation of molten carbonic anhydrase during thermal unfolding and refolding. Proteins 37: 321324.
  • Kuwajima, K., Ikeguchi, M., Sugawara, T., Hiraoka, Y., and Sugai, S. 1990. Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the cys6-cys120 disulfide bond. Biochemistry 29: 82408249.
  • Lan, E.H., Dave, B.C., Fukuto, J.M., Dunn, B., Zink, J.I., and Valentine, J.S. 1999. Synthesis of sol-gel encapsulated heme proteins with chemical sensing properties. J. Mater. Chem. 9: 4553.
  • Minton, A.P. 1981. Excluded volume as a determinant of macromolecular structure and reactivity. Biopolymers 20: 20932120.
  • Minton, A.P. 1992. Confinement as a determinant of macromolecular structure and reactivity. Biophys. J. 63: 10901100.
  • Minton, A.P. 1995. Confinement as a determinant of macromolecular structure and reactivity. II. Effects of weakly attractive interactions between confined macrosolutes and confining structures. Biophys. J. 68: 13111322.
  • Minton, A.P. 2000. Effect of concentrated “inert” macromolecule cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: A statistical-thermodynamic model. Biophys. J. 78: 101109.
  • Pace, C.N., Shirley, B.A., and Thomson, J.A. 1990. Measuring the conformational stability of a protein. In Protein structure: A practical approach (ed. T.E.Creighton), pp. 311330. IRL Press, Oxford, UK.
  • Reetz, M.T., Zonta, A., Simpelkamp, J., Rufinska, A., and Tesche, B. 1996. Characterization of hydrophobic sol-gel materials containing entrapped lipases. J. Sol-Gel Sci. Technol. 7: 3543.
  • Rozema, D. and Gellman, S.H. 1996. Artificial chaperone-assisted refolding of carbonic anhydrase B. J. Biol. Chem. 271: 34783487.
  • Schmid, F.X. 1990. Spectral methods of characterizing protein conformation and conformational changes. In Protein structure: A practical approach (ed. T.E.Creighton), pp. 251285. IRL Press, Oxford, UK.
  • Shen, C. and Kostic, N.M. 1997. Kinetics of photoinduced electron-transfer reactions within sol-gel silica glass doped with zinc cytochrome c. Study of electrostatic effects in confined liquids. J. Am. Chem. Soc. 119: 13041312.
  • Shiraki, K., Nishikawa, K., and Goto, Y. 1995. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-heirarchical protein folding. J. Mol. Biol. 245: 180194.
  • Shtelzer, S., Rappoport, S., Avnir, D., Ottolenghi, M., and Braun, S. 1992. Properties of trypsin and of acid phosphatase immobilized in sol-gel glass matrices. Biotechnol. Appl. Biochem. 15: 227235.
  • Soper, A.K., Bruni, F., and Ricci, M.A. 1998. Water confined in Vycor glass. II. Excluded volume effects on the radial distribution functions. J. Chem. Phys. 109: 14861494.
  • Sreerama, N. and Woody, R.W. 1993. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209: 3244.
  • Teixeira, J., Zanotti, J.M., Bellissent-Funel, M.C., and Chen, S.H. 1997. Water in confined geometries. Physica B 234–236: 370374.
  • Tellam, R.L., Sculley, M.J., Nichol, W., and Wills, P.R. 1983. The influence of poly(ethylene glycol) 6000 on the properties of skeletal-muscle actin. Biochem. J. 213: 651659.
  • van den Berg, B., Ellis, R.J., and Dobson, C.M. 1999. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18: 69276933.
  • van den Berg, B., Wain, R., Dobson, C.M., and Ellis, R.J. 2000. Macromolecular crowding perturbs protein refolding kinetics: Implications for folding inside the cell. EMBO J. 19: 38703875.
  • von Hippel, P.H. and Wong, K.-Y. 1964. Neutral salts: The generality of their effects on the stability of macromolecular conformations. Science 145: 577580.
  • Wiggins, P.M. 1997. Hydrophobic hydration, hydrophobic forces, and protein folding. Physica A 238: 113128.
  • Zheng, L. and Brennan, J.D. 1998. Measurement of intrinsic fluorescence to probe the conformational stability and thermodynamic stability of a single tryptophan protein entrapped in a sol-gel derived glass matrix. Analyst 123: 17351744.
  • Zheng, L., Flora, K., and Brennan, J.D. 1998. Improving the performance of a sol-gel entrapped metal-binding protein by maximizing protein thermal stability before entrapment. Chem. Mater. 10: 39743983.
  • Zimmerman, S.B. and Trach, S.O. 1991. Estimation of macromolecular concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J. Mol. Biol. 222: 599620.
  • Zimmerman, S.B. and Minton, A.P. 1993. Macromolecular crowding: Biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22: 2765.