Conformational Study of Spectrin in Presence of Submolar Concentrations of Denaturants
暂无分享,去创建一个
[1] A. Chakrabarti,et al. Membrane interaction of erythroid spectrin: Surface-density-dependent high-affinity binding to phosphatidylethanolamine , 2004, Molecular membrane biology.
[2] M. Haque,et al. Polarity Estimate of the Hydrophobic Binding Sites in Erythroid Spectrin: A Study by Pyrene Fluorescence , 2000, Journal of Fluorescence.
[3] A. Chakrabarti,et al. Organization and dynamics of tryptophan residues in erythroid spectrin: Novel structural features of denatured spectrin revealed by the wavelength‐selective fluorescence approach , 2003, Protein science : a publication of the Protein Society.
[4] A. Chakrabarti,et al. Erythroid spectrin in miceller detergents. , 2003, Cell motility and the cytoskeleton.
[5] Alfonso Mondragón,et al. Structures of Two Repeats of Spectrin Suggest Models of Flexibility , 1999, Cell.
[6] S. Basak,et al. Structural changes of horseradish peroxidase in presence of low concentrations of urea. , 1999, European journal of biochemistry.
[7] M. Morris,et al. Biophysical properties of human erythrocyte spectrin at alkaline pH: implications for spectrin structure, function, and association. , 1998, Biochemistry.
[8] Anders Wallqvist,et al. HYDROPHOBIC INTERACTIONS IN AQUEOUS UREA SOLUTIONS WITH IMPLICATIONS FOR THE MECHANISM OF PROTEIN DENATURATION , 1998 .
[9] M Nilges,et al. Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil. , 1997, Journal of molecular biology.
[10] D. Pantazatos,et al. Site-directed Mutagenesis of Either the Highly Conserved Trp-22 or the Moderately Conserved Trp-95 to a Large, Hydrophobic Residue Reduces the Thermodynamic Stability of a Spectrin Repeating Unit* , 1997, The Journal of Biological Chemistry.
[11] S. Basak,et al. Structural alterations of horseradish peroxidase in the presence of low concentrations of guanidinium chloride. , 1996, European journal of biochemistry.
[12] A. Chakrabarti. Fluorescence of spectrin-bound prodan. , 1996, Biochemical and biophysical research communications.
[13] D. Sackett,et al. Charge-shielding and the "paradoxical" stimulation of tubulin polymerization by guanidine hydrochloride. , 1996, Biochemistry.
[14] Gottfried Otting,et al. Specificity of Urea Binding to Proteins , 1994 .
[15] M. Saraste,et al. Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[16] R. Macdonald,et al. Fluorescence studies of spectrin and its subunits. , 1994, Cell motility and the cytoskeleton.
[17] D. Branton,et al. Crystal structure of the repetitive segments of spectrin. , 1993, Science.
[18] G. Ralston,et al. The self-association of ovine erythrocyte spectrin. , 1993, The International journal of biochemistry.
[19] P. Privalov,et al. Protein interactions with urea and guanidinium chloride. A calorimetric study. , 1992, Journal of molecular biology.
[20] E. Kahana,et al. Fluorescence quenching of spectrin and other red cell membrane cytoskeletal proteins. Relation to hydrophobic binding sites. , 1992, The Biochemical journal.
[21] J. Schellman. A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures. , 1990, Biophysical chemistry.
[22] Andreas Matouschek,et al. Transient folding intermediates characterized by protein engineering , 1990, Nature.
[23] V. Marchesi,et al. Full-length sequence of the cDNA for human erythroid beta-spectrin. , 1990, The Journal of biological chemistry.
[24] D. Speicher,et al. The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin. , 1990, The Journal of biological chemistry.
[25] M. Mooseker,et al. Contributions of the β‐subunit to spectrin structure and function , 1989 .
[26] A. Sikorski,et al. Interaction of spectrin with phospholipids. Quenching of spectrin intrinsic fluorescence by phospholipid suspensions. , 1987, Biochimica et biophysica acta.
[27] V. Marchesi,et al. Isolation of spectrin subunits and reassociation in vitro. Analysis by fluorescence polarization. , 1984, The Journal of biological chemistry.
[28] J. Lakowicz. Principles of fluorescence spectroscopy , 1983 .
[29] W. Gratzer. [44] Preparation of spectrin , 1982 .
[30] S. N. Timasheff,et al. Interactions of proteins with solvent components in 8 M urea. , 1981, Archives of biochemistry and biophysics.
[31] M. Eftink,et al. Fluorescence quenching studies with proteins. , 1981, Analytical biochemistry.
[32] N. Green,et al. Binding of hydrophobic ligands to spectrin , 1981, FEBS letters.
[33] E. Ungewickell,et al. A conformational study of human spectrin. , 2005, European journal of biochemistry.
[34] G. Weber,et al. Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-propionyl-2-(dimethylamino)naphthalene. , 1979, Biochemistry.
[35] D M Shotton,et al. The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies. , 1979, Journal of molecular biology.
[36] A. Elgsaeter. Human spectrin. I. A classical light scattering study. , 1978, Biochimica et biophysica acta.
[37] S. Lehrer,et al. [10] Solute quenching of protein fluorescence , 1978 .
[38] D. Branton,et al. Selective association of spectrin with the cytoplasmic surface of human erythrocyte plasma membranes. Quantitative determination with purified (32P)spectrin. , 1977, The Journal of biological chemistry.
[39] G. Edelman,et al. Fluorescent probes for conformational states of proteins. IV. The pepsinogen-pepsin conversion. , 1971, The Journal of biological chemistry.
[40] C. Tanford. Protein denaturation. , 1968, Advances in protein chemistry.
[41] J. S. Coleman,et al. Physical Chemistry of Protein Solutions. VII. The Binding of Some Small Anions to Serum Albumin1 , 1957 .
[42] O. H. Lowry,et al. Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.