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  Section: General Biochemistry » Protein Folding
 
 
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Bibliography of Protein Folding

 
     
 
Hynes, T. R., and Fox, R. O. (1991). “The crystal structure of staphylococcal nuclease refined at 1.7 A resolution,” Proteins Struct. Funct. Genet. 10, 92–105.

Kraulis , P. J. (1991). “MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures,” J. Appl. Crystallogr. 24, 946–950.

Laurents, D. V., and Baldwin, R. L. (1998). “Protein Folding: Matching Theory and Experiment” Biophysical J. 75, 428–434.

Privalov, P. L., and Gill, S. J. (1988). “Stability of protein structure and hydrophobic interaction,” Adv. Protein Chem. 39, 191–234.

Lin, L. N., and Brandts, J. F. (1988). “Separation of the nativelike intermediate from unfolded forms during refolding of ribonuclease A,” Biochemistry 27, 9037–9042.

Schellman, J. A. (1987). “The thermodynamic stability of proteins,” Ann. Rev. Biophys. Biophys. Chem. 16, 115–137.

Becktel, W. J., and Schellman, J. A. (1987). “Protein stability curves,” Biopolymers 26, 1859–1876.

Privalov, P. L. (1990). “Cold denaturation of proteins,” Crit. Rev. Biochem. 25, 281–305.

Schellman, J. A. (1978). “Solvent denaturation,” Biopolymers 17, 1305–1322.

Pace, C. N. (1986). “Determination and analysis of urea and guanidine hydrochloride denaturation curves,” Methods Enzymol. 131, 266–280.

Santoro, M. M., and Bolen, W. D. (1992). “Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants,” Biochemistry 31, 8063–8068.

Palidini, A. A., andWeber, G. (1981). “Pressure induced reversible dissociation of enolase,” Biochemistry 20, 2587–2593.

Silva, J. L., andWeber, G. (1993). “Pressure stability of proteins,” Annu. Rev. Phys. Chem. 44, 89–113.

Schmid, F. X. (1989). “Spectral methods of characterizing protein conformation and conformational changes,” In “Protein Structure: A Practical Approach” (T. E. Creighton, ed.), pp. 251–285, IRL Press, Oxford.

Andrews, L. J., and Forster, L. S. (1972). “Protein difference spectra. Effect of solvent and charge on tryptophan,” Biochemistry 11, 1875– 1879.

Eftink, M. R. (1995). “Use of multiple spectroscopic methods to monitor the equilibrium unfolding of proteins,” Methods Enzymol. 259, 487– 512.

Johnson,W. C. (1988). “Secondary structure of proteins through circular dichroism spectroscopy,” Ann. Rev. Biophys. Biophys. Chem. 17, 145– 166.

Yu, S., Venyaminiov, S. Y., and Yang, J. T. (1996). “Determination of protein secondary structure,” In “Circular Dichroism and the Conformational Analysis of Biomolecules” (G. D. Fasman, ed.), pp. 69–107, Plenum Press, New York.

Eftink, M. R. (1996). “Fluorescence techniques for studying protein structure,” Methods Biochem. Anal. 35, 127–205.

Eftink, M. R. (1994). “The use of fluorescence to monitor unfolding transitions in proteins,” Biophys. J. 66, 482–501.

Lakowicz, J. R. (200). “Protein fluorescence,” In “Topics in Fluorescence Spectroscopy,” Vol. 6, Plenum Press, New York.

Haugland, R. P. (1983). “Covalent fluorescent probes,” In “Excited States of Biopolymers” (R. F. Steiner, ed.) pp. 29–58, Plenum Press, New York.

Sturtevant., J. M. (1897). “Biochemical applications of differential scanning calorimetry,” Ann. Rev. Phys. Chem. 38, 463–488.

Biltonen, R. L., and Freire, E. (1978). “Thermodynamic characterization of conformational states of biological macromolecules using differential scanning calorimetry,” CRC Critical Rev. Biochem. 5, 85–124.

Cooper, A., and Johnson, C. M. (1994). “Differential scanning microcalorimetry,” Methods Molec. Biol. 22, 125–136.

Roder,H. (1989). “Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange,” Methods Enzymol. 176, 446–473.

Englander, W., and Mayne, L. (1992). “Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR,” Ann. Rev. Biochem. Biophys. Chem. 21, 243–265.

Muga, A., Mantsch, H. H., and Surewicz, W. K. (1991). “Membrane binding induces destabilization of cytochrome c structure,” Biochemistry 30, 7219–7224.

Nicoli, D. F., and Benedek, G. B. (1976). “Study of thermal denaturation of lysozyme and other glubular proteins by light-scattering spectroscopy,” Biopolymers 15, 2421–2437.

Corbett, R. T., and Roche, R. S. (1984). “Use of high-speed sizeexclusion chromatography for the study of protein folding and stability,” Biochemistry 23, 1888–1894. Creighton, T. E. (1980). “Kinetic study of protein unfolding and refolding using urea gradient electrophoresis,” J. Mol. Biol. 137, 61–80.

Hilser, V. J., Worosila, G. D., and Freire, E. (1993). “Analysis of thermally induced protein folding/unfolding transitions using free solution capillary electrophoresis,” Anal. Biochem. 208, 125–131.

Dandliker, W. B., Dandliker, J., Levison, S. A., Kelley, R. J., Hicks, A. N., and White, J. U. (1978). “Fluorescence methods for measuring reaction equilibria and kinetics,” Methods Enzymol. 48, 380–415.

Eftink, M. R., and Shastry, M. R. C. (1997). “Fluorescence methods for studying kinetics of protein folding reactions,” Methods Enzymol. 278, 258–287.

Utiyama, H., and Baldwin, R. L. (1986). “Kinetic mechanisms of protein folding,” Methods Enzymol. 131, 51–70.

Schmid, F. X. (1992). “Kinetics of unfolding and refolding of singledomain proteins,” In “Protein Folding” (T. E. Creighton, ed.), pp. 197–241, W. H. Freeman, New York.

 
     
 
 
     



     
 
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