Stability of folded conformations

Current Opinion in Structural Biology - Tập 1 - Trang 5-16 - 1991
Thomas E. Creighton1
1European Molecular Biology Laboratory, Posffach 10.2209, Meyerhofstrasse 1, D-6900, Heidelberg, FRG

Tài liệu tham khảo

Privalov, 1989, Thermodynamic Problems of Protein Structure, Annu Rev Biophys Biophys Chem, 18, 47, 10.1146/annurev.bb.18.060189.000403 Dill, 1990, Dominant Forces in Protein Folding, Biochemistry, 29, 7133, 10.1021/bi00483a001 Murphy, 1990, Common Features of Protein Unfolding and Dissolution of Hydrophobic Compounds, Science, 247, 559, 10.1126/science.2300815 Kauzmann, 1959, Some Factors in the Interpretation of Protein Denaturation, Adv Protein Chem, 14, 1, 10.1016/S0065-3233(08)60608-7 Privalov, 1990, Science, 250, 297, 10.1126/science.250.4978.297-a Privalov PL: Stability of Proteins. Small Globular Proteins. Adv Protein Chem 179, 33: 167–241. Privalov, 1988, Stability of Protein Structure and Hydrophobic Interaction, Adv Protein Chem, 39, 191, 10.1016/S0065-3233(08)60377-0 Privalov, 1989, The Hydrophobic Effect: A Reappraisal, Pure Appl Chem, 61, 1097, 10.1351/pac198961061097 Baldwin, 1986, Temperature Dependence of the Hydrophobic Interaction in Protein Folding, 83, 8069 Spolar, 1989, Hydrophobic Effect in Protein Folding and Other Noncovalent Processes Involving Proteins, 86, 8382 Rao, 1989, Hydrophobic Hydration: A Free Energy Perturbation Study, J Am Chem Soc, 111, 3125, 10.1021/ja00191a003 Linse, 1990, Molecular Dynamics Simulation of a Dilute Aqueous Solution of Benzene, J Am Chem Soc, 112, 1744, 10.1021/ja00161a014 Muller, 1990, Search for a Realistic View of Hydrophobic Effects, Acc Chem Res, 23, 23, 10.1021/ar00169a005 Makhatadze, 1990, Heat Capacity of Proteins. I. Partial Molar Heat Capacity of Individual Amino Acid Residues in Aqueous Solution: Hydration Effect, J Mol Biol, 213, 375, 10.1016/S0022-2836(05)80197-4 Privalov, 1990, Heat Capacity of Proteins. II. Partial Molar Heat Capacity of the Unfolded Polypeptide Chain of Proteins, J Mol Biol, 213, 385, 10.1016/S0022-2836(05)80198-6 Privalov, 1989, Heat Capacity and Conformation of Proteins in the Denatured State, J Mol Biol, 205, 737, 10.1016/0022-2836(89)90318-5 Dill, 1989, Thermal Stabilities of Globular Proteins, Biochemistry, 28, 5439, 10.1021/bi00439a019 Stigter, 1990, Charge Effects on Folded and Unfolded Proteins, Biochemistry, 29, 1262, 10.1021/bi00457a023 Privalov, 1990, Cold Denaturation of Proteins, Crit Rev Biochem, 25, 281, 10.3109/10409239009090612 Shinoda, 1977, ‘Iceberg’ Formation and Solubility, J Phys Chem, 81, 1300, 10.1021/j100528a016 Pohorille, 1990, Cavities in Molecular Liquids and the Theory of Hydrophobic Solubilities, J Am Chem Soc, 112, 5066, 10.1021/ja00169a011 Arnold, 1988, Protein Design for Non-Aqueous Solvents, Protein Eng, 2, 21, 10.1093/protein/2.1.21 Burke, 1989, Demonstration of Structural Integrity of an Enzyme in Organic Solvents by Solid-State NMR, J Am Chem Soc, 111, 8290, 10.1021/ja00203a046 Fujita, 1981, Effect of Hydration on the Thermal Stability of Protein as Measured by Differential Scanning Calorimetry. Chymotrypsinogen A, Int J Pept Protein Res, 18, 12, 10.1111/j.1399-3011.1981.tb02034.x Rees, 1989, The Bacterial Photosynthetic Reaction Center as a Model for Membrane Proteins, Annu Rev Biochem, 58, 607, 10.1146/annurev.bi.58.070189.003135 Rees, 1989, Hydrophobic Organization of Membrane Proteins, Science, 245, 510, 10.1126/science.2667138 Ooi, 1988, Effects of Hydrated Water on Protein Unfolding, J Biochem, 103, 114, 10.1093/oxfordjournals.jbchem.a122215 Oobatake, 1988, Characteristic Thermodynamic Properties of Hydrated Water for 20 Amino Acid Residues in Globular Proteins, J Biochem, 104, 433, 10.1093/oxfordjournals.jbchem.a122485 Khechinashvili, 1990, Thermodynamic Properties of Globular Proteins and the Principle of Stabilization of Their Native Structure, Biochim Biophys Acta, 1040, 346, 10.1016/0167-4838(90)90132-Y Creighton, 1983, An Empirical Approach to Protein Conformation Stability and Flexibility, Biopolymers, 22, 49, 10.1002/bip.360220110 Bello, 1977, Stability of Protein Conformation: Internal Packing and Enthalpy of Fusion of Model Compounds, J Theor Biol, 68, 139, 10.1016/0022-5193(77)90232-6 Burley, 1989, Electrostatic Interactions in Aromatic Oligopeptides Contribute to Protein Stability, Trends Biotechnol, 7, 354, 10.1016/0167-7799(89)90036-X Murphy, 1989, Thermodynamics of Dissolution of Solid Cyclic Dipeptides Containing Hydrophobic Side Groups, J Chem Thermodyn, 21, 903, 10.1016/0021-9614(89)90149-3 Murphy, 1990, Group Additivity Thermodynamics for Dissolution of Solid Cyclic Dipeptides into Water, Thermochim Acta, 10.1016/0040-6031(90)80555-D Wolfenden, 1983, Waterlogged Molecules, Science, 222, 1087, 10.1126/science.6359416 Hawkes, 1984, Thermodynamic Stability and Point Mutations of Bacteriophage T4 Lysozyme, J Mol Biol, 175, 195, 10.1016/0022-2836(84)90474-1 Shortle, 1988, Stability Mutants of Staphylococcal Nuclease: Large Compensating Enthalpy-Entropy Changes for the Reversible Denaturation Reaction, Biochemistry, 27, 4761, 10.1021/bi00413a027 Kitamura, 1989, A Scanning Calorimetric Study of the Thermal Denaturation of the Lysozyme of Phage T4 and the Arg 96→ His Mutant From Thereof, Biochemistry, 28, 3788, 10.1021/bi00435a024 Kelly, 1990, A Comparative Study of the Unfolding Thermodynamics of Vertebrate Metmyoglobins, Biochemistry, 29, 5062, 10.1021/bi00473a010 Karpusas, 1989, Hydrophobic Packing in T4 Lysozyme Probed by Cavity-Filling Mutants, 86, 8237 Perutz, 1975, Stereochemical Basis of Heat Stability in Bacterial Ferredoxin and in Haemoglobin A2, Nature, 255, 256, 10.1038/255256a0 McLinden, 1986, Mechanism of Thermophily for Thermolabile Glyceraldehyde-3-Phosphate Dehydrogenase from the Facultative Thermophile Bacillus Coagulans KU, Biochim Biophys Acta, 871, 207, 10.1016/0167-4838(86)90175-5 Frömel, 1989, Thermitase, a Thermostable Subtilisin: Comparison of Predicted and Experimental Structures and the Molecular Cause of Thermostability, Proteins, 5, 22, 10.1002/prot.340050105 Doig, 1991, Is the Hydrophobic Effect Stabilising or Destabilising in Proteins? The Contribution of Disulphide Bonds to Protein Stability, J Mol Biol, 10.1016/0022-2836(91)90551-G Schwartz, 1987, Stability Studies on Derivatives of the Bovine Pancreatic Trypsin Inhibitor, Biochemistry, 26, 3544, 10.1021/bi00386a044 Shortle, 1989, Residual Structure in Large Fragments of Staphylococcal Nuclease: Effects of Amino Acid Substitutions, Biochemistry, 28, 936, 10.1021/bi00429a003 Bowie, 1990, Deciphering the Message in Protein Sequences: Tolerance to Amino Acid Substitutions, Science, 247, 1306, 10.1126/science.2315699 Lim, 1989, Alternative Packing Arrangements in the Hydrophobic Core of Lambda Repressor, Nature, 339, 31, 10.1038/339031a0 Sandberg, 1989, Influence of Interior Packing and Hydrophobicity on the Stability of a Protein, Science, 245, 54, 10.1126/science.2787053 Kells, 1989, Energetics of Complementary Side-Chain Packing in a Protein Hydrophobic Core, Biochemistry, 28, 4914, 10.1021/bi00437a058 Pakula, 1990, Reserve Hydrophobic Effects Relieved by Amino Acid Substitutions at a Protein Surface, Nature, 344, 363, 10.1038/344363a0 Fersht, 1987, The Hydrogen Bond in Molecular Recognition, Trends Biochem Sci, 12, 301, 10.1016/0968-0004(87)90146-0 Fersht, 1988, Relationships Between Apparent Binding Energies Measured in Site-Directed Mutagenesis Experiments and Energetics of Binding and Catalysis, Biochemistry, 27, 1577, 10.1021/bi00405a027 Timasheff, 1990, Stabilization of Protein Structure by Solvents, 331 Arakawa, 1990, Preferential Interactions Determine Protein Solubility in Three-Component Solutions: the MgCl2 System, Biochemistry, 29, 1914, 10.1021/bi00459a036 Arakawa, 1990, Why Preferential Hydration does not always Stabilize the Native Structure of Globular Proteins, Biochemistry, 29, 1924, 10.1021/bi00459a037 Arakawa, 1984, Protein Stabilization and Destabilization by Guanidium Salts, Biochemistry, 23, 5924, 10.1021/bi00320a005 Breslow, 1990, Surface Tension Measurements Show that Chaotropic Salting-in Denaturants are not just Water-Structure Breakers, 87, 167 Lehmann, 1989, Binding of Dimethyl Sulfoxide to Lysozyme in Crystals, Studied with Neutron Diffraction, Biochemistry, 28, 7028, 10.1021/bi00443a037 Hibbard, 1978, Expression of Functionality of α-Chymotrypin. Effects of Guanidine Hydrochloride and Urea in the Onset of Denaturation, Biochemistry, 17, 5460, 10.1021/bi00618a021 Pace, 1990, Measuring and Increasing Protein Stability, Trends Biotechnol, 8, 93, 10.1016/0167-7799(90)90146-O Kuroki, 1989, Design and Creation of a Ca2+ Binding Site in Human Lysozyme to Enhance Structural Stability, 86, 6903 Shrake, 1990, Ligand-Induced Biphasic Protein Denaturation, J Biol Chem, 265, 5055, 10.1016/S0021-9258(19)34083-9 Pace, 1990, pH Dependence of the Urea and Guanidine Hydrochloride Denaturation of Ribonuclease A and Ribonuclease T1, Biochemistry, 29, 2564, 10.1021/bi00462a019 Shortle, 1986, Mutant Forms of Staphylococcal Nuclease with Altered Patterns of Guanidine Hydrochloride and Urea Denaturation, Proteins, 1, 81, 10.1002/prot.340010113 Shortle, 1990, Contributions of the Large Hydrophobic Amino Acids to the Stability of Staphylococcal Nuclease, Biochemistry, 29, 8033, 10.1021/bi00487a007 Zaccai, 1989, Stabilization of Halophilic Malate Dehydrogenase, J Mol Biol, 208, 491, 10.1016/0022-2836(89)90512-3 Zaccai, 1990, Halophilic Proteins and the Influence of Solvent on Protein Stabilization, Trends Biochem Sci, 15, 333, 10.1016/0968-0004(90)90068-M Sharp, 1990, Electrostatic Interactions in Macromolecules: Theory and Applications, Annu Rev Biophys Biophys Chem, 19, 301, 10.1146/annurev.bb.19.060190.001505 Stigter, 1990, Charge Effects on Folded and Unfolded Proteins, Biochemistry, 29, 1262, 10.1021/bi00457a023 Perry, 1989, Long-Range Electrostatic Interactions can Influence the Folding Stability, and Cooperativity of Dihydrofolate Reductase, Biochemistry, 28, 7961, 10.1021/bi00445a061 Akke, 1990, Protein Stability and Electrostatic Interactions Between Solvent Exposed Charged Side Chains, Proteins, 8, 23, 10.1002/prot.340080106 Hollecker, 1982, Effect on Protein Stability of Reversing the Charge on Amino Groups, Biochim Biophys Acta, 701, 395, 10.1016/0167-4838(82)90243-6 Goto, 1990, Acid-Induced Folding of Proteins, Proc Natl Acad Sci USA, 87, 573, 10.1073/pnas.87.2.573 Goto, 1990, Mechanism of Acid-Induced Folding of Proteins, Biochemistry, 29, 3480, 10.1021/bi00466a009 Kelly, 1990, Conformational Free Energy of Armadillo Metmyoglobin, Int J Pept Protein Res, 35, 235, 10.1111/j.1399-3011.1990.tb00943.x McNutt, 1990, Contribution of Histidine Residues to the Conformational Stability of Ribonuclease T1 and Mutant Glu-58→Ala, Biochemistry, 29, 7572, 10.1021/bi00485a005 Anderson, 1990, pH-Induced Denaturation of Proteins — a Single Salt Bridge Contributes 3–5 kcal/mol to the Free Energy of Folding of T4-Lysozyme, Biochemistry, 29, 2403, 10.1021/bi00461a025 Roseman, 1988, Extension of the Fragment Method, to Calculate Amino Acid Zwitterion and Side Chain Partition Coefficients, J Mol Biol, 201, 621, 10.1016/0022-2836(88)90642-0 Abraham, 1987, Hydrophobicity of the Peptide CO…H-N Hydrogen-Bonded Group, Proteins, 2, 130, 10.1002/prot.340020207