Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of Thermus thermophilus ribonuclease H.
暂无分享,去创建一个
Srebrenka Robic | Antonio Parody-Morreale | S. Marqusee | J. M. Sanchez-Ruiz | S. Robic | Susan Marqusee | Mercedes Guzman-Casado | Jose M Sanchez-Ruiz | A. Parody-Morreale | M. Guzmán-Casado
[1] R. Alberty. Maxwell relations for thermodynamic quantities of biochemical reactions , 1969 .
[2] P. Privalov,et al. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. , 1974, Journal of molecular biology.
[3] W. J. Becktel,et al. Protein stability curves , 1987, Biopolymers.
[4] A hydrophobic cluster forms early in the folding of dihydrofolate reductase , 1989, Proteins.
[5] P. Privalov,et al. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect. , 1990, Journal of molecular biology.
[6] P. Privalov,et al. Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range , 1990, Biopolymers.
[7] C. Dobson,et al. Hydrophobic clustering in nonnative states of a protein: Interpretation of chemical shifts in NMR spectra of denatured states of lysozyme , 1991, Proteins.
[8] R. S. Spolar,et al. Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. , 1992, Biochemistry.
[9] G. Wider,et al. NMR determination of residual structure in a urea-denatured protein, the 434-repressor. , 1992, Science.
[10] S. Marqusee,et al. Equilibrium unfolding of Escherichia coli ribonuclease H: Characterization of a partially folded state , 1994, Protein science : a publication of the Protein Society.
[11] P. Privalov,et al. Thermodynamics of staphylococcal nuclease denaturation. II. The A‐state , 1994, Protein science : a publication of the Protein Society.
[12] P. S. Kim,et al. Formation of a hydrophobic cluster in denatured bovine pancreatic trypsin inhibitor. , 1994, Journal of molecular biology.
[13] D. Xie,et al. Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease , 1994, Protein science : a publication of the Protein Society.
[14] P. Privalov,et al. Thermodynamics of staphylococcal nuclease denaturation. I. The acid‐denatured state , 1994, Protein science : a publication of the Protein Society.
[15] V. Hilser,et al. The heat capacity of proteins , 1995, Proteins.
[16] J. M. Sanchez-Ruiz,et al. An osmolyte effect on the heat capacity change for protein folding. , 1995, Biochemistry.
[17] J. Udgaonkar,et al. Initial hydrophobic collapse in the folding of barstar , 1995, Nature.
[18] P. Privalov,et al. Energetics of protein structure. , 1995, Advances in protein chemistry.
[19] E. Freire,et al. Differential scanning calorimetry. , 2008, Methods in cell biology.
[20] J. M. Sanchez-Ruiz. Differential scanning calorimetry of proteins. , 1995, Sub-cellular biochemistry.
[21] B. Shirley,et al. Protein Stability and Folding: Theory and Practice , 1995 .
[22] C. Matthews,et al. Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. , 1996, Biochemistry.
[23] A. Mozzarelli,et al. Time-resolved fluorescence of tryptophan synthase. , 1996, Biophysical chemistry.
[24] V V Plotnikov,et al. A new ultrasensitive scanning calorimeter. , 1997, Analytical biochemistry.
[25] A. Fersht,et al. The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. , 1997, Journal of molecular biology.
[26] I. Luque,et al. Structure-based prediction of binding affinities and molecular design of peptide ligands. , 1998, Methods in enzymology.
[27] P. D. W. Pfeil. Protein Stability and Folding , 1998, Springer Berlin Heidelberg.
[28] J. Otlewski,et al. Structure of single-disulfide variants of bovine pancreatic trypsin inhibitor (BPTI) as probed by their binding to bovine beta-trypsin. , 1998, Journal of molecular biology.
[29] D. Raleigh,et al. Peptide models of local and long-range interactions in the molten globule state of human alpha-lactalbumin. , 1998, Journal of molecular biology.
[30] Steady state and time-resolved fluorescence study of residual structures in an unfolded form of yeast phosphoglycerate kinase. , 1998, Biochemistry.
[31] S Marqusee,et al. Molten globule unfolding monitored by hydrogen exchange in urea. , 1998, Biochemistry.
[32] M. Sudol,et al. WW: An isolated three‐stranded antiparallel β‐sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state , 2008, Protein science : a publication of the Protein Society.
[33] J. Beechem,et al. Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. , 1999, Biochemistry.
[34] C. Dobson,et al. Side-chain conformations in an unfolded protein: chi1 distributions in denatured hen lysozyme determined by heteronuclear 13C, 15N NMR spectroscopy. , 1999, Journal of molecular biology.
[35] C. Matthews,et al. The progressive development of structure and stability during the equilibrium folding of the α subunit of tryptophan synthase from Escherichia coli , 1999, Protein science : a publication of the Protein Society.
[36] E. Freire,et al. A simple method to measure the absolute heat capacity of proteins. , 1999, Analytical biochemistry.
[37] S. Marqusee,et al. A thermodynamic comparison of mesophilic and thermophilic ribonucleases H. , 1999, Biochemistry.
[38] A. Elcock. Realistic modeling of the denatured states of proteins allows accurate calculations of the pH dependence of protein stability. , 1999, Journal of molecular biology.
[39] G. Makhatadze,et al. Cold denaturation of ubiquitin. , 1999, Biochimica et biophysica acta.
[40] H. Hinz,et al. A new set of peptide-based group heat capacities for use in protein stability calculations. , 1999, Journal of molecular biology.
[41] Kevin L. Shaw,et al. Charge–charge interactions influence the denatured state ensemble and contribute to protein stability , 2000, Protein science : a publication of the Protein Society.
[42] H. Dyson,et al. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. , 2001, Biochemistry.
[43] D. Shortle,et al. Persistence of Native-Like Topology in a Denatured Protein in 8 M Urea , 2001, Science.
[44] J. Sancho,et al. Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate. , 2001, Journal of molecular biology.
[45] M. L. Tasayco,et al. Heat capacity analysis of oxidized Escherichia coli thioredoxin fragments (1--73, 74--108) and their noncovalent complex. Evidence for the burial of apolar surface in protein unfolded states. , 2001, European journal of biochemistry.
[46] Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies. , 2001, Biochemistry.
[47] M. M. Garcia-Mira,et al. pH corrections and protein ionization in water/guanidinium chloride. , 2001, Biophysical journal.
[48] M. M. Garcia-Mira,et al. pH corrections in chemical denaturant solutions. , 2002, Analytical biochemistry.
[49] Petras J Kundrotas,et al. Modeling of denatured state for calculation of the electrostatic contribution to protein stability , 2002, Protein science : a publication of the Protein Society.
[50] R. L. Baldwin,et al. Making a Network of Hydrophobic Clusters , 2002, Science.
[51] Huan-Xiang Zhou,et al. A Gaussian-chain model for treating residual charge–charge interactions in the unfolded state of proteins , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[52] K. Crowhurst,et al. Cooperative interactions and a non-native buried Trp in the unfolded state of an SH3 domain. , 2002, Journal of molecular biology.
[53] Lorna J. Smith,et al. Long-Range Interactions Within a Nonnative Protein , 2002, Science.