Molecular confinement influences protein structure and enhances thermal protein stability
Article first published online: 31 DEC 2008
Copyright © 2001 The Protein Society
Volume 10, Issue 2, pages 250–261, February 2001
How to Cite
Eggers, D. K. and Valentine, J. S. (2001), Molecular confinement influences protein structure and enhances thermal protein stability. Protein Science, 10: 250–261. doi: 10.1110/ps.36201
- Issue published online: 31 DEC 2008
- Article first published online: 31 DEC 2008
- Manuscript Accepted: 9 NOV 2000
- Manuscript Revised: 2 NOV 2000
- Manuscript Received: 30 AUG 2000
- 1967. Reversible denaturation of sperm whale myoglobin. I. Dependence on temperature, pH, and composition. J. Am. Chem. Soc. 89: 1543–1552. and
- 1999. Effects of encapsulation in sol-gel silica glass on esterase activity, conformational stability, and unfolding of bovine carbonic anhydrase II. Chem. Mater. 11: 3671–3679. and
- 1996. How Hofmeister ion interactions affect protein stability. Biophys. J. 71: 2056–2063.
- 1990. Biochemically active sol-gel glasses: The trapping of enzymes. Materials Lett. 10: 1–5. , , , , and
- 1995. Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl. Acad. Sci. 92: 6229–6233. , , , and
- 1997. Charge density-dependent strength of hydration and biological structure. Biophys. J. 72: 65–76.
- 1985. The Hofmeister effect and the behavior of water at interfaces. Q. Rev. Biophys. 18: 323–422. and
- 1994. Sol-gel encapsulation methods for biosensors. Anal. Chem. 66: 1120A–1127A. , , , and
- 1994. Vibrational spectra of water molecules at quartz/water interfaces. Phys. Rev. Lett. 72: 238–241. , , and
- 1994. Spectroscopic characterization of albumin and myoglobin entrapped in bulk sol-gel glasses. J. Colloid Interface Sci. 163: 395–406. , , , and
- 1992. Encapsulation of proteins in transparent porous silicate glasses prepared by the sol-gel method. Science 255: 1113–1115. , , , , , , and
- 1997. Molecular chaperones: Avoiding the crowd. Curr. Biol. 7: R531–R533.
- 1993. Structural characterization of the disulfide folding intermediates of bovine α-lactalbumin. Biochemistry 32: 3694–3707. and
- 1999. Trifluoroethanol-induced conformational transitions of proteins: Insights gained from the differences between α-lactalbumin and ribonuclease A. Protein Sci. 8: 625–634. , , , and
- 1990. Phase diagram for acidic conformational states of apomyoglobin. J. Mol. Biol. 214: 803–805. and
- 1999. Impeded rotation of a protein in a sol-gel matrix. J. Phys. Chem. B 103: 2803–2807. , , , and
- 1968. Comparison of myoglobins from harbor seal, porpoise, and sperm whale. J. Biol. Chem. 243: 683–689. , , , and
- 1999. Co-translational folding. Curr. Op. Struct. Biol. 9: 111–114. , , and
- 1997. Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci. 6: 416–421. , , and
- 1999. Microwave dielectric relaxation of bound water to silica, alumina, and silica-alumina gel suspensions. J. Colloid Interface Sci. 212: 144–151. and
- 1996. Comparison of adsorption and conformation of hemoglobin and myoglobin on various inorganic ultrafine particles. J. Colloid Interface Sci. 177: 214–221. and
- 1999. Hydrophobic dye inhibits aggregation of molten carbonic anhydrase during thermal unfolding and refolding. Proteins 37: 321–324. and
- 1990. Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the cys6-cys120 disulfide bond. Biochemistry 29: 8240–8249. , , , , and
- 1999. Synthesis of sol-gel encapsulated heme proteins with chemical sensing properties. J. Mater. Chem. 9: 45–53. , , , , , and
- 1981. Excluded volume as a determinant of macromolecular structure and reactivity. Biopolymers 20: 2093–2120.
- 1992. Confinement as a determinant of macromolecular structure and reactivity. Biophys. J. 63: 1090–1100.
- 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: 1311–1322.
- 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: 101–109.
- 1990. Measuring the conformational stability of a protein. In Protein structure: A practical approach (ed. T.E.Creighton), pp. 311–330. IRL Press, Oxford, UK. , , and
- 1996. Characterization of hydrophobic sol-gel materials containing entrapped lipases. J. Sol-Gel Sci. Technol. 7: 35–43. , , , , and
- 1996. Artificial chaperone-assisted refolding of carbonic anhydrase B. J. Biol. Chem. 271: 3478–3487. and
- 1990. Spectral methods of characterizing protein conformation and conformational changes. In Protein structure: A practical approach (ed. T.E.Creighton), pp. 251–285. IRL Press, Oxford, UK.
- 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: 1304–1312. and
- 1995. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-heirarchical protein folding. J. Mol. Biol. 245: 180–194. , , and
- 1992. Properties of trypsin and of acid phosphatase immobilized in sol-gel glass matrices. Biotechnol. Appl. Biochem. 15: 227–235. , , , , and
- 1998. Water confined in Vycor glass. II. Excluded volume effects on the radial distribution functions. J. Chem. Phys. 109: 1486–1494. , , and
- 1993. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209: 32–44. and
- 1997. Water in confined geometries. Physica B 234–236: 370–374. , , , and
- 1983. The influence of poly(ethylene glycol) 6000 on the properties of skeletal-muscle actin. Biochem. J. 213: 651–659. , , , and
- 1999. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18: 6927–6933. , , and
- 2000. Macromolecular crowding perturbs protein refolding kinetics: Implications for folding inside the cell. EMBO J. 19: 3870–3875. , , , and
- 1964. Neutral salts: The generality of their effects on the stability of macromolecular conformations. Science 145: 577–580. and
- 1997. Hydrophobic hydration, hydrophobic forces, and protein folding. Physica A 238: 113–128.
- 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: 1735–1744. and
- 1998. Improving the performance of a sol-gel entrapped metal-binding protein by maximizing protein thermal stability before entrapment. Chem. Mater. 10: 3974–3983. , , and
- 1991. Estimation of macromolecular concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J. Mol. Biol. 222: 599–620. and
- 1993. Macromolecular crowding: Biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22: 27–65. and