Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity

Quarterly Reviews of Biophysics

Volumn 11, Issue 2, 1978, Pages 103-178

  Record Jr, M Thomas ^a   Anderson, Charles F ^a   Lohman, Timothy M ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEIC ACID; PROTEIN;

NONBIOLOGICAL MODEL;

IONS; LIGANDS; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; THERMODYNAMICS;

EID: 0017820499     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S003358350000202X     Document Type: Article

References (154)

1. Anderson, C. F., Record, M. T., Jr & Hart, P. A. (1978). Sodium-23 NMR studies of cation-DNA interactions. Biophysical Chem. 7, 301–316
2. Antonini, E. & Brunori, M. (1971). Hemoglobin and Myoglobin in Their Reactions with Ligands. Amsterdam: North Holland
3. Aune, K. C. & Tanford, C. (1969 a). Thermodynamics of the dénaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 250. Biochemistry, N.Y. 8, 4579–4585
4. Aune, K. C. & Tanford, C. (1969). Thermodynamics of the dénaturation of lysozyme by guanidine hydrochloride. II. Dependence on dénaturant concentration at 25°. Biochemistry, N.Y. 8, 4586–4590
5. Aune, K. C., Goldsmith, L. C. & Timasheff, S. N. (1971). Dimerization of a-chymotrypsin. II. Ionic strength and temperature dependence. Biochemistry, N.Y. 10, 1617–1622
6. Aune, K. C. & Timasheff, S. N. (1971). Dimerization of a-chymotrypsin. I. pH dependence in the acid region. Biochemistry, N.Y. 10, 1609–1617
7. Benesch, R. E., Benesch, R. & Yu, C. I. (1969). The oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength and hemoglobin concentration. Biochemistry, N. Y. 8, 2567–2571
8. Berg, D. & Chamberlin, M. (1970). Physical studies on RNA polymerase from E. coli B. Biochemistry, N.Y. 9, 5055–5064
9. Bloomfield, V. A., Crothers, D. M. & Tinoco, I. (1974). Physical Chemistry of Nucleic Acids. New York: Harper and Row
10. Bradbury, E. M., Cary, P. D., Crave-Robinson, D., Rattle, H. W. E. & Boublik, M. (1975). Conformations and interactions of histone H2A (F2A2, ALK). Biochemistry, N.Y. 14, 1876–1885
11. Bradley, D. F. & Lifson, S. (1968). Statistical mechanical analysis of binding of acridines to DNA. In Molecular Associations in Biology (ed. B. Pullman), pp. 261–270. New York: Academic Press
12. Breslauer, K. J., Sturtevant, J. M. & Tinoco, I., Jr. (1975). Calorimetric and spectroscopic investigation of the helix-to-coil transition of a ribo-oligonucleotide: rA7U7. J. molec. Biol. 99, 549–565
13. Brun, F., Toulmjé, J. & Hélène, C. (1975). Interactions of aromatic residues of proteins with nucleic acids. Fluorescence studies of the binding of oligopeptides containing tryptophan and tyrosine residues to polynucleotides. Biochemistry, N.Y. 14, 558–563
14. Carr, C. W. (1955). Determination of ionic activity in protein solutions with collodion membrane electrodes. In Electrochemistry in Biology and Medicine (ed. T. Shedlovsky), 266–283. New York: Wiley
15. Chiancone, E., Norne, J. E., Forsén, S., Antonini, E. & Wyman, J. (1972). Nuclear magnetic resonance quadrupole relaxation studies of chloride binding to human oxy- and deoxyhemoglobin. J. molec. Biol. 70, 675— 688
16. Chiancone, E., Norne, J. E., Forsén, S., Bonaventura, J., Brunori, M., Antonini, E. & Wyman, J. (1975). Identification of chloride-binding sites in hemoglobin by nuclear-magnetic-resonance quadrupole relaxation studies of hemoglobin digests. Eur. J. Biochem. 55, 385–390
17. Chiancone, E., Norne, J. E., Forsén, S., Mansouri, A. & Winterhalter, K. H. (1976). Anion binding to proteins. NMR quadrupole relaxation study of chloride binding to various human hemoglobins. FEBS Lett. 63, 309–312
18. Crothers, D. M. (1971). Statistical thermodynamics of nucleic acid melting transitions with coupled binding equilibria. Biopolymers 10, 2147–2160
19. D'Anna, J. A. & Isenberg, I. (1974). Conformational changes of histone LAK (1972). Biochemistry, N.Y. 2093–2098
20. Daune, M. P. (1972). Interactions protéines-acides nucléiques. 1. Étude theorique de l'association. Eur. J. Biochem. 26, 207–211
21. Davidson, S. J. & Jencks, W. P. (1969). The effect of concentrated salt solutions on a merocyanine dye, a vinglogous amide. J. Am. chem. Soc. 91, 225–234
22. deHaseth, P. L., Lohman, T. M. & Record, M. T., Jr. (1977). Nonspecific interaction of lac repressor with DNA: An association reaction driven by counterion release. Biochemistry, N. Y. 16, 4783–4790
23. deHaseth, P. L. Lohman, T. M., Burgess, R. R. & Record, M. T., Jr. (1978). Interactions of E. coli RNA polymerase with native and denatured DNA: Differences in the binding behavior of core and holoenzyme. Biochemistry, N.Y. 17, 1612–1622
24. Draper, D. E. & Von Hippel, P. H. (1978a). Nucleic acid binding properties of E. coli ribosomal protein Si. I. Structure and interactions of binding site I. J. molec. Biol. (In the Press.)
25. Draper, D. E. & Von Hippel, P. H. (1978). Nucleic acid binding properties of E. coli ribosomal protein Si. II. Cooperativity and specificity of binding site II. J. molec. Biol. (In the Press.)
26. Durand, M., Maurizot, J. C., Borazan, H. N. & Hélène, C. (1975). Interaction of aromatic residues of proteins with nucleic acids. Circular dichroism studies of the binding of oligopeptides to poly(adenylic acid). Biochemistry, N.Y. 14, 563–570
27. Dwek, R. A. (1973). Nuclear Magnetic Resonance in Biochemistry. Oxford: Clarendon Press
28. Eisenberg, H. (1974). Hydrodynamic and thermodynamic studies. In Basic Principles in Nucleic Add Chemistry, vol. 11 (ed. P. O. P. Ts'o), pp. 171-264. New York: Academic Press
29. Elson, E. L., Scheffler, I. E. & Baldwin, R. L. (1970). Helix formation by d(TA) oligomers. III. Electrostatic effects. J. molec. Biol. 54, 401–415
30. Felsenfeld, G. & Miles, H. T. (1967). The physical and chemical properties of nucleic acids. A. Rev. Biochem. 36, 407–448
31. Friedberg, F. (1974). Effects of metal binding on protein structure. Q. Rev. Biophys. 7, 1–33
32. Friedberg, F. & Bose, S. (1969). Ion binding by α-chymotrypsin. Biochemistry, N.Y. 8, 2564–2567
33. Friedberg, F. & Emiola, L. O. (1968). Ion binding by metmyoglobin. Biochemistry, N.Y. 7, 2183–2185
34. Frigon, R. P. & Timasheff, S. N. (1975). Magnesium-induced self association of calf brain tubulin. II. Thermodynamics. Biochemistry, N.Y. 14,4567–4573
35. Gillberg-La Force, G. & Forsén, S. (1970). The binding of anionic surfactants to human serum albumin studied by means of 81Br nuclear magnetic resonance. Biochem. biophys. Res. Commun 38, 137–142
36. Greene, R. F., Jr. & Pace, C. N. (1974). Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, a-chymotrypsin. and β lacto-globulin. J. biol. Chem. 249, 5388–5393
37. Gruenwedel, P. W. & Hsu, C. H. (1969). Salt effects on the denaturation of DNA. Biopolymers 7, 557–570
38. Guidotti, G. (1967). Studies on the chemistry of hemoglobin. II. The effect of salts on the dissociation of hemoglobin into subunits. J. biol. Chem. 242, 3685–3693
39. Haire, R. N. & Hedlund, B. E. (1977). Thermodynamic aspects of the linkage between binding of chloride and oxygen to human hemoglobin. Proc. natn. Acad. Sci. U.S.A. 74, 4135–4138
40. Hamabata, A. & Von Hippel, P. H. (1973). Model studies on the effects of neutral salts on the conformational stability of biological macromolecules. II. Effects of vicinal hydrophobic groups on the specificity of binding of ions to amide groups. Biochemistry, N.Y. 12, 1264–1271
41. Hamabata, A., Chang, S. & Von Hippel, P. H. (1973). Model studies on the effects of neutral salts on the conformational stability of biological macromolecules. III. Solubility of fatty acid amides in ionic solutions. Biochemistry, N.Y. 12, 1271–1278
42. Hamaguchi, K. & Geiduschek, E. P. (1962). The effect of electrolytes on the stability of the deoxyribonucleate helix. J. Am. chem. Soc. 84, 1329–1338
43. Herskovits, T. T., Cavanagh, S. M. & San George, R. D. (1977). Light-scattering investigations of the subunit dissociation of human hemoglobin. A. Effects of various neutral salts. Biochemistry, N.Y. 16, 5795–5801
44. Ibanez, V. S. & Herskovits, T. T. (1976). Effects of the aliphatic carboxylate series of salts on the conformation of proteins. Biochemistry, N.Y. 15,5708–5714
45. Jencks, W. P. (1969). Catalysis in Chemistry and Enzymology. New York: McGraw-Hill
46. Jensen, D. E., Kelly, R. C. & Von Hippel, P. H. (1976). DNA melting proteins. II. Effects of bacteriophage T4 gene-32 protein binding on the conformation and stability of nucleic acid structures. J. biol. Chem. 251, 7215–7228
47. Jensen, D. E. & Von Hippel, P. H. (1976). DNA'melting'proteins. I. Effects of bovine pancreatic ribonuclease binding on the conformation and stability of DNA. J. biol. Chem. 251, 7198–7214
48. Jonas, A. & Weber, G. (1971). Presence of arginine residues at the strong, hydrophobic anion binding sites of bovine serum albumin. Biochemistry, N.Y. 10, 1335–1339
49. Josephs, R. & Harrington, W. F. (1968). On the stability of myosin filaments. Biochemistry, N. Y. 7, 2834–2847
50. Katsura, I. & Noda, H. (1973). Further studies on the formation of reconstituted myosin filaments. J. Biochem (Tokyo) 73, 245–256
51. Kellett, G. L. (1971). Dissociation of hemoglobin into subunits: Ligandlinked dissociation at neutral pH. J. molec. Biol. 59, 401–424
52. Kirshner, A. G. & Tanford, C. (1964). The dissociation of hemoglobin by inorganic salts. Biochemistry, N.Y. 3, 291–296
53. Klotz, I. M. (1953). Protein interactions. In The Proteins, vol. iB (ed. H. Neurath and K. Bailey), pp. 727–806. New York: Academic Press
54. Klotz, I. M., Darnall, D. W. & Langerman, N. R. (1975). Quaternary structure of proteins. In The Proteins, vol. 1, 3rd ed. (ed. H. Neurath and R. L. Hill), pp. 294–411. New York: Academic Press
55. Klotz, I. M. & Urquhart, J. M. (1949). The binding of organic ions by proteins. Buffer effects. J. Phys. Chem. 53, 100–114
56. Klump, H. & Ackermann, T. (1971). Experimental thermodynamics of the helix-random coil transition. IV. Influence of the base composition, of the DNA on the transition enthalpy. Biopolymers 10, 513–522
57. Knapp, J. A. & Pace, C. N. (1974). Guanidine hydrochloride and acid dénaturation of horse, cow, and Candida krusei cytochromes C. Biochemistry, N.Y. 13, 1289–1294
58. Kotin, L. (1963). On the effect of ionic strength on the melting temperature of DNA. J. molec. Biol. 7, 309–311
59. Krakauer, H. (1974). A thermodynamic analysis of the influence of simple monovalent and divalent cations on the conformational transitions of polynucleotide complexes. Biochemistry, N. Y. 13, 2579–2589
60. Krakauer, H. & Sturtevant, J. M. (1968). Heats of the helix-coil transitions of the polyA-polyU complexes. Biopolymers 6, 491–512
61. Latt, S. A. & Sober, H. A. (1967). Protein-nucleic acid interactions. II. Oligopeptide-polyribonucleotide binding studies. Biochemistry, N.Y. 6, 3293–3306
62. Lee, J. C. & Timasheff, S. N. (1977). In vitro reconstitution of calf brain microtubules: Effect of solution variables. Biochemistry, N.Y. 16, 1754–1764
63. Lewis, M. S. & Saroff, H. A. (1957). The binding of ions to the muscle proteins. Measurements on the binding of potassium and sodium ions to myosin A, myosin B, and actin. J. Am. chem. Soc. 79, 2112–2117
64. Lifson, S. (1964). Partition functions of linear-chain molecules. J. chem. Phys. 40. 3705–3710
65. Lindman, B. & Forsén, S. (1976). Chlorine, Bromine and Iodine NMR. Berlin: Springer-Verlag
66. Lindman, B., Kamenka, N. & Brun, B. (1972). Detergent translational mobility in the presence of human serum albumin. Biochim. biophys. Acta. 285, 118–123
67. Loeb, G. I. & Saroff, H. A. (1964). Chloride- and hydrogen-ion binding to ribonuclease. Biochemistry, N.Y. 3, 1819–1826
68. Lohman, T. M. & Record, M. T., Jr. (1978). (In preparation.)
69. Lohman, T. M., Wensley, C. G. & Record, M. T., Jr. (1978). (In preparation.)
70. Long, F. A. & McDevit, W. F. (1952). Activity coefficients of nonelectrolyte solutes in aqueous salt solutions. Chem. Revs. 51, 119–169
71. Longsworth, L. G. & Jacobsen, C. F. (1949). An electrophoretic study of the binding of salt ions by /?-lactoglobulin and bovine serum albumin. J. Phys. Chem. 53, 126–135
72. Losick, R. & Chamberlin, M. (eds.) (1976). RNA Polymerase. New York: Cold Spring Harbor Press
73. Mandelkern, L. & Stewart, W. E. (1964). The effect of neutral salts on the melting temperature and regeneration kinetics of the ordered collagen structure. Biochemistry, N.Y. 3, 1135–1137
74. Manning, G. S. (1969). Limiting laws and counterion condensation in polyelectrolyte solutions. I. Colligative properties. J. chem. Phys. 51,924–933
75. Manning, G. S. (1972a). On the application of polyelectrolyte ‘limiting laws’ to the helix-coil transition of DNA. I. Excess univalent cations. Biopolymers 11, 937–949
76. Manning, G. S. (1972). On the application of polyelectrolyte ‘limiting laws’ to the helix-coil transition of DNA. II. The effect of Mg++ counterions. Biopolymers n, 951–955
77. Manning, G. S. (1974). Limiting laws for equilibrium and transport properties of polyelectrolyte solutions. In Polyelectrolytes (ed. E. Selegny), pp. 9–38. Holland: Reidel
78. Manning, G. S. (1975). Remarks on the paper ‘Nuclear magnetic relaxation of 23Na in polyelectrolyte solutions’ by van der Klink, Zuiderweg and Leyte. J. chem. Phys. 62, 748–749
79. Manning, G. S. (1976). The application of polyelectrolyte limiting laws to the helix-coil transition of DNA. VI. The numerical value of the axial phosphate spacing for the coil. Biopolymers 15, 2385–2390
80. Manning, G. S. (1978). The molecular theory’ of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Q. Rev. Biophys. 11, 179–246
81. Manning, G. S. & Holtzer, A. (1973). Application of polyelectrolyte limiting laws to potentiometric titration. J. Phys. Chem. 77, 2206–2212
82. McGhee, J. D. (1976). Theoretical calculations of the helix-coil transition of DNA in the presence of large cooperatively binding ligands. Biopolymers 15. 1345–1375
83. McGhee, J. D. & Von Hippel, P. H. (1974). Theoretical aspects of DNA-pro-tein interactions: cooperative and non-cooperative binding of large ligands to a one dimensional homogeneous lattice. J. molec. Biol. 86, 469–489
84. Mukerjee, P. (1965). Salt effects on nonionic association colloids. J. Phys. Chem. 69, 4038–4040
85. Nakanishi, M., Tsuboi, M. & Ikegani, A. (1973). Fluctuation of the lysozyme structure. II. Effects of temperature and binding of inhibitors. J. molec. Biol. 75, 673–682
86. Nandi, P. K. & Robinson, D. R. (1972 a). The effects of salts on the free energy of the peptide group. J. Am. chem. Soc. 94, 1299–1308
87. Nandi, P. K. & Robinson, D. R. (1972). The effects of salts on the free energies of nonpolar groups in model peptides. J. Am. chem. Soc. 94, 1308–1315
88. Nelson, C. A., Hummel, J. P., Swenson, C. A. & Friedman, L. (1962). Stabilization of pancreatic ribonuclease against urea dénaturation by anion binding. J. biol. Chem. 237, 1575–1580
89. Norne, J. E., Hjalmarsson, S. G., Lindman, B. & Zeppezauer, M. (1975a). Anion binding properties of human serum albumin from halide ion quadrapole relaxation. Biochemistry, N. Y. 14, 3401–3408
90. Norne, J. E., Lilja, H., Lindman, B., Einarsson, R. & Zeppezauer, M. (1975). Pt(CN)42˜ and Au(CN)2_: Potential general probes for anion-binding sites of proteins. 36C1 and 81Br NMR studies. Eur. J. Biochem. 59, 463–473
91. Olson, W. K. & Manning, G. S. (1976). A configurational interpretation of the axial phosphate spacing in polynucleotide helices and random coils. Biopolymers 15, 2391–2405
92. Oosawa, F. (1971). Poly electrolytes. New York: Marcel Dekker
93. Pande, C. S. & McMenamy, R. H. (1970). Thiocyanate binding with modified bovine plasma albumins. Archs Biochem. Biophys. 136, 260–267
94. Passero, F., Gabbay, E. J., Gaffney, B. & Kurucsev, T. (1970). Topography of nucleic acid helices in solutions. Stoichiometry and specificity of the interaction of reporter molecules with nucleic acid helices. Macromolecules 3, 158–162
95. Pfeil, W. & Privalov, P. L. (1976a). Thermodynamic investigation of proteins. I. Standard functions for protein with lysozyme as an example. Biophys. Chem. 4, 23–32
96. Pfeil, W. & Privalov, P. L. (1976). Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme dénaturation by guanidine hydrochloride. Biophys. Chem. 4, 33–40
97. Pfeil, W. & Privalov, P. L. (1976 c). Thermodynamic investigations of proteins. III. Thermodynamic description of lysozyme. Biophys. Chem. 4. 41–50
98. Poliakow, M. C., Champagne, M. H. & Daune, M. P. (1972). Interactions protéines-acides nucléiques 2. Étude de l'association d'histones riches en lysine avec la DNA. Eur. J. Biochem. 26, 212–219
99. Privalov, P. L. & Khechinashvili, N.N. (1974). A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study. J. molec. Biol. 86, 665–684
100. Privalov, P. L., Ptitsyn, O. B. & Birshtein, T. M. (1969). Determination of stability of the DNA double helix in an aqueous medium. Biopolymers 8, 559–571
101. Puett, D. (1973). The equilibrium unfolding parameters of horse and sperm whale myoglobin. Effects of guanidine hydrochloride, urea, and acid. J. biol. Chem. 248, 4623–4634
102. Record, M. T., Jr. (1967a). Polyelectrolyte effects on polynucleotide transitions. I. Behavior at neutral pH. Biopolymers 5, 975–992
103. Record, M. T., Jr. (1967). Polyelectrolyte effects on polynucleotide transitions. II. Behavior of titrated systems. Biopolymers 5, 993–1008
104. Record, M. T., Jr. (1975). Effects of Na+ and Mg++ on the helix-coil transition of DNA. Biopolymers 14, 2137–2158
105. Record, M. T., Jr., deHaseth, P. L. & Lohman, T. M. (1977). Interpretation of monovalent and divalent ion effects on the lac repressor-operator interaction. Biochemistry, N.Y. 16, 4791–4796
106. Record, M. T., Jr. & Lohman, T. M. (1978). A semi-empirical extension of polyelectrolyte theory to the treatment of oligoelectrolytes. Application to oligonucleotide helix-coil transitions. Biopolymers 17, 159–166
107. Record, M. T., Jr., Lohman, T. M. & deHaseth, P. L. (1976a). Ion effects on ligand-nucleic acid interactions. J. molec. Biol. 107, 145–158
108. Record, M. T., Jr., Woodbury, C. P. & Lohman, T. M. (1976). Na+ effects on transitions of DNA and polynucleotides of variable linear charge density. Biopolymers 15, 893–915
109. Reuben, J. & Gabbay, E. J. (1975). Binding of manganese(n) to DNA and the competitive effects of metal ions and organic cations. An electron paramagnetic resonance study. Biochemistry, N.Y. 14, 1230–1235
110. Reuben, J., Shporer, M. & Gabbay, E. J. (1975). The alkali-ion-DNA interaction as reflected in the nuclear relaxation rates of 23Na and 87Rb. Proc. natn. Acad. Sci. U.S.A. 72, 245–247
111. Revzin, A. & Von Hippel, P. H. (1977). Direct measurement of association constants for the binding of Escherichia coli lac repressor to non-operator DNA. Biochemistry, N.Y. 16, 4769–4776
112. Richards, F. & Wyckoff, H. (1971). Bovine pancreatic ribonuclease. In The Proteins, vol. 4 (ed. P. D. Boyer), pp. 647–806
113. Riggs, A. (1971). Mechanism of the enhancement of the Bohr effect in mammalian hemoglobins by diphosphoglycerate. Proc. natn. Acad. Sci. U.S.A. 68, 2062–2065
114. Riggs, A. D., Bourgeois, S. & Cohn, M. (1970). The lac repressor-operator interaction. III. Kinetic studies. J. molec. Biol. 53, 401–417
115. Riggs, A. D., Suzuki, H. & Bourgeois, S. (1970a). Lac repressor-operator interaction. I. Equilibrium Studies. J. molec. Biol. 48, 67–83
116. Rix-Montel, M. A., Grassi, H. & Vasilescu, D. (1974). Experimental studies of thermal denaturation of the Na-DNA system with respect to Manning's model. Biophys. Chem. 2, 278–289
117. Rix-Montel, M. A., Grassi, A. & Vasilescu, D. (1976). Dielectric study of the interaction between DNA and an oligopeptide (lysine-tyrosine-lysine). Nucl. Acids Res. 3, 1001–1011
118. Robinson, D. R. & Grant, M. E. (1966). The effects of aqueous salt solutions on the activity coefficients of purine and pyrimidine bases and their relation to the denaturation of deoxyribonucleic acid by salts. J. biol. Chem. 241, 4030–4042
119. Robinson, D. R. & Jencks, W. P. (1965a). The effect of concentrated salt solutions on the activity coefficient of acetyltetraglycine ethyl ester. J. Am. chem. Soc. 87, 2470–2479
120. Robinson, D. R. & Jencks, W. P. (1965). The effect of compounds of the urea-guanidinium class on the activity coefficient of acetyltetraglycine ethyl ester and related compounds. J. Am. chem. Soc. 87, 2462–2470
121. Robinson, R. A. & Stokes, R. H. (1959). Electrolyte Solutions, 2nd ed. London: Butterworths
122. Rollema, H. S., De Bruin, S. H., Janssen, L. H. M. & Van Os, G. A. S. (1975). The effect of potassium chloride on the Bohr effect of human hemoglobin. J. biol. Chem. 250, 1333–1339
123. Salahuddin, A. & Tanford, C. (1970). Thermodynamics of the dénaturation of ribonuclease by guanidine hydrochloride. Biochemistry, N. Y. 9, 1342–1347
124. Saroff, H. A. & Carroll, W. R. (1962). The binding of chloride and sulfate ions to ribonuclease. J. biol. Chem. 237, 3384–3387
125. Saucier, J.-M. (1977). Physicochemical studies on the interaction of irehdiamine A with bihelical DNA. Biochemistry, N.Y. 16, 5879–5889
126. Scatchard, G. (1949). The attractions of proteins for small molecules and ions. Ann. N.Y. Acad. Sci. 51, 660–672
127. Scatchard, G. & Black, E. S. (1949). The effects of salts on the isoionic and isoelectric points of proteins. J. Phys. Chem. 53, 88–99
128. Scatchard, G. & Yap, W. T. (1964). The physical chemistry of protein solutions. XII. The effects of temperature and hydroxide ion on the binding of small anions to human serum albumin. J. Am. chem. Soc. 86, 3434–3438
129. Schellman, J. (1974). Cooperative multi-site binding to DNA. Israel Jnl Chem. 12, 219–238
130. Schellman, J. (1975). Macromolecular binding. Biopolymers 14, 999–1018
131. Schildkraut, C. & Lifson, S. (1965). Dependence of the melting temperature of DNA on salt concentration. Biopolymers 3, 195–208
132. Schrier, E. E. & Schrier, E. B. (1967). The salting-out behavior of amides and its relation to the dénaturation of proteins by salts. J. Phys. Chem. 71, 1851–1860
133. Shiao, D. D. F. & Sturtevant, J. M. (1973). Heats of thermally induced helix-coii transitions of DNA in aqueous solution. Biopolymers 12, 1829–1836
134. Steinhardt, J. & Beychok, S. (1964). Interaction of proteins with hydrogen ions and other small ions and molecules. In The Proteins (ed. H. Neurath), pp. 140–304. New York: Academic Press
135. Steinhardt, J. & Reynolds, J. A. (1969). Multiple Equilibria in Proteins. New York: Academic Press
136. Suelter, C. H. (1974). Monovalent cations in enzyme-catalyzed reactions. In Metal Ions in Biological Systems, vol. 3 (ed. H. Sigel). Vol. 3. High Molecular Weight Complexes, pp. 201–251. New York: Marcell Dekker
137. Tanford, C. (1969). Extension of the theory of linked functions to incorporate the effects of protein hydration. J. molec. Biol. 39, 539–544
138. Tanford, C. & Aune, K. C. (1970). Thermodynamics of the dénaturation of lysozyme by guanidine hydrochloride. III. Dependence on temperature. Biochemistry, N.Y. 9, 206–211
139. Taylor, R. P. & Kuntz, I. D., Jr. (1972). Proton acceptor abilities of anions and possible relevance to the Hofmeister series. J. Am. chem. Soc. 94, 7963–7965
140. Thomas, J. O. & Edelstein, S. (1973). Observation of the dissociation of unliganded hemoglobin. II. Effect of pH, salt and dioxane. J. biol. Chem. 248, 2901–2905
141. Valdes, R. & Ackers, G. K. (1977). Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (αSH and βsn): Determination of stoichiometries and equilibrium constants as a function of temperature. J. biol. Chem. 252, 74–81
142. Van der Klink, J. J., Zuiderweg, L. H. & Leyte, J. D. (1974). Nuclear magnetic relaxation of 23Na in polyelectrolyte solutions. J. chem. Phys. 60, 2391-2399; 62, 749 (1975)
143. Von Hippel, P. H. & McGhee, J. D. (1972). DNA-protein interactions. A. Rev. Biochem. 41, 231–300
144. Von Hippel, P. H., Peticolas, V., Schack, L. & Karlson, L. (1973). Model studies on the effects of neutral salts on the conformational stability of biological macromolecules. I. Ion binding to polyacrylamide and polystyrene columns. Biochemistry, N.Y. 12, 1256–1264
145. Von Hippel, P. H. & Schleich, T. (1969a). The effects of neutral salts on the structure and conformational stability of macromolecules in solution. In Biological Macromolecules. Vol. 2. Structure and Stability of Biological Macromolecules (ed. S. N. Timasheff and G. Fasman), pp. 417–574. New York: Marcel Dekker
146. Von Hippel, P. H. & Schleich, T. (1969). Ion effects on the solution structure of biological macromolecules. Acc. Chem. Res. 2, 257–265
147. Von Hippel, P. H. & Wong, K. Y. (1962). The effects of ions on the kinetics of formation and the stability of the collagen-fold. Biochemistry, N. Y. 1, 664–674
148. Von Hippel, P. H. & Wong, K. Y. (1965). On the conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition. J. biol. Chem. 240, 3909–3923
149. Wang, J. C. & Davidson, N. (1966). Thermodynamic and kinetic studies on the interconversion between the linear and circular forms of phage lambda DNA. J. molec. Biol. 19, 469–482
150. Wang, J. C. & Davidson, N. (1968). Cyclization of phage DNAs. Cold Spring Harb. Symp. quant. Biol. 33, 409–415
151. Wensley, C. G. & Record, M. T., Jr. (1978). (In preparation.)
152. Wickett, R. R., Li, H. S. & Isenberg, I. (1972). Salt effects on histone IV conformation. Biochemistry, N.Y. 11, 2952–2957
153. Wyman, J. (1948). Heme proteins. Adv. Protein Chem. 4, 407–531
154. Wyman, J. (1964). Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19, 223–286