Thermodynamic stability of ribonuclease a in alkylurea solutions and preferential solvation changes accompanying its thermal denaturation: A calorimetric and spectroscopic study

Protein Science

Volumn 8, Issue 4, 1999, Pages 832-840

  Poklar, Nataša ^a   Petrovčič, Nina ^a   Oblak, Miha ^a   Vesnaver, Gorazd ^a  

^a UNIVERSITY OF LJUBLJANA   (Slovenia)

Author keywords

CD spectropolarimetry; Denatured states; Differential scanning calorimetry; Preferential solvation changes; Ribonuclease A; Thermal and solvent denaturation; UV spectroscopy

Indexed keywords

RIBONUCLEASE A; UREA DERIVATIVE;

ARTICLE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME DENATURATION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; SOLVATION; STRUCTURE ANALYSIS; TEMPERATURE; THERMODYNAMICS; THERMOSTABILITY; ULTRAVIOLET SPECTROSCOPY;

EID: 0345040176     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.4.832     Document Type: Article

References (51)

1. Barone G, Rizzo E, Volpe V. 1972. Osmotic and activity coefficients of alkylureas in water at 25°C. J Chem Eng Data 21:59-61.
2. Bierzynski A, Baldwin RL. 1982. Local secondary structure in ribonuclease A denatured by guanidine HCl near 1°C. J Mol Biol 162:173-186.
3. Bychkova VE, Dujsekina AE, Klenin SI, Tiktopulo EI, Uversky VN, Ptitsyn OB. 1996. Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry 35:6058-6063.
4. Dunbar J, Yennawar HP, Banerjee S, Luo J, Farber GK. 1997. The effect of denaturants on protein structure. Protein Sci 6:1727-1733.
5. Fabian H, Mantsch HH. 1995. Ribonuclease A revisited: Infrared spectroscopic evidence for lack of native-like secondary structures in the thermally denatured state. Biochemistry 34:13651-13655.
6. Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR. 1994. Classification of acid denaturation of proteins. Intermediates and unfolded states. Biochemistry 33:12504-12511.
7. Freer ST, Kraut J, Robertus JD, Wright HT, Xuong NgH. 1970. Chymotrypsinogen: 2.5-Å crystal structure, comparison with α-chymotrypsin, and implications for zymogen activation. Biochemistry 9:1997-2009.
8. Fujita Y, Noda Y. 1991. Effect of reductive alkylation on thermal stability of ribonuclease A and chymotrypsinogen A. Int J Pept Protein Res 38:445-452.
9. Ginsburg A, Carroll WR. 1965. Some specific ion effects on the conformation and thermal stability of ribonuclease. Biochemistry 4:2159-2174.
10. Gordon JA, Jencks WP. 1963. The relationship of structure to the effectiveness of denaturing agents for proteins. Biochemistry 2:47-57.
11. Green RF, Pace CN. 1974. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotripsin, and β-lactoglobulin. J Biol Chem 249:5388-5393.
12. Haynie DT, Freire E. 1994. Estimation of the folding/unfolding energetics of marginally stable proteins using differential scanning calorimetry. Anal Biochem 216:33-41.
13. Hirota N, Mizuno K, Goto Y. 1997. Cooperative alpha-helix formation of beta-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci 6:416-421.
14. Houry WA, Rotwarf DM, Scheraga HA. 1996. Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A. Biochemistry 35:10125-10133.
15. Jayaraman G, Kumar TKS, Arunkumar AI, Yu C. 1996. 2,2,2-Trifluoroethanol induces helical conformation in an all β-sheet protein. Biochem Bioph Res Co 222:33-37.
16. Kamatari YO, Konno T, Kataoka M, Akasaka K. 1996. The methanol-induced globular and expanded denatured states of cytochrome C: A study by CD, fluorescence, NMR and small-angle X-ray scattering. J Mol Biol 259:512-523.
17. Kovrigin EL, Potekhin SA. 1997. Preferential solvation changes upon lysozyme heat denaturation in mixed solvents. Biochemistry 36:9195-9199.
18. Kugimiya M, Bigelow CC. 1973. Denatured states of lysozyme. Can J Biochem 51:581-585.
19. Labhardt AM. 1982. Secondary structure in ribonuclease. II. Relations between folding kinetics and secondary structure elements. J Mol Biol 157:331-355.
20. Lapanje S, Kranjc Z. 1982. Interactions of β-lactoglobulin with some alkylureas. Biochim Biophys Acta 705:111-116.
21. Lapanje S, Poklar N. 1989. Calorimetric and CD studies of the thermal denaturation of β-lactoglobulin. Biophys Chem 34:155-162.
22. Lapanje S, Simič M, Pavlič A. 1981. Interaction of α-chymotrypsinogen A with some alkylureas. Croat Chem Acta 54:481-488.
23. Liu Y, Sturtevant JM. 1996. The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding. Biochemistry 35:3059-3062.
24. Makhatadze GI, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride: A calorimetric study. J Mol Biol 226:491-505.
25. Marky LA, Breslauer KJ. 1987. Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves. Biopolymers 26:1601-1620.
26. Pace N. 1992. Contribution of the hydrophobic effect to globular protein stability. J Mol Biol 226:29-35.
27. Plaza del Pino IM, Sanchez-Ruiz JM. 1995. An osmolyte effect on the heat capacity change for protein folding. Biochemistry 34:8621-8630.
28. Poklar N, Lan J, Salobir M, Maček P, Vesnaver G. 1997. pH and temperature-induced molten globule-like denatured states of equinatoxin II: A study by UV-melting, DSC, far-and near-UV CD spectroscopy, and ANS fluorescence. Biochemistry 36:14345-14352.
29. Poklar N, Lapanje S. 1992. Solvation of β-lactoglobulin in alkylurea solutions. Biophys Chem 42:283-290.
30. Poklar N, Vesnaver G, Lapanje S. 1993. Studies by UV spectroscopy of thermal denaturation of β-lactoglobulin in urea and alkylurea solutions. Biophys Chem 47:143-151.
31. Poklar N, Vesnaver G, Lapanje S. 1995. Thermodynamics of denaturation of α-chymotrypsinogen A with alkylureas. J Protein Chem 14:709-719.
32. Poklar N, Vesnaver G, Lapanje S. 1996. Interactions of α-chymotrypsinogen A with alkylureas. Biophys Chem 57:279-289.
33. Privalov PL, Khechinashvili NN. 1974. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study. J Mol Biol 86:665-684.
34. Privalov PL, Makhatadze GI. 1992. Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding. J Mol Biol 213:385-391.
35. Reinställer D, Fabian H, Backmann J, Naumann D. 1996. Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy. Biochemistry 35:15822-15830.
36. Scatchard G. 1946. Physical chemistry of protein solutions. I. Derivation of the equations for the osmotic pressure. J Am Chem Soc 68:2315-2319.
37. Schellman JA. 1978. Solvent denaturation. Biopolymers 17:1305-1322.
38. Schellman JA. 1990. A simple model for solvation in mixed solutions. Biophys Chem 37:121-140.
39. Schellman JA. 1993. The relation between the free energy of interaction and binding. Biophys Chem 45:273-279.
40. Schellman JA. 1994. The thermodynamics of solvent exchange. Biopolymers 34:1015-1026.
41. Scheraga HA. 1967. Structural studies of pancreatic ribonuclease. Fed Proc 26:1380-1387.
42. Schrier EE, Ingwall RT, Scheraga HA. 1965. The effect of aqueous alcohol solutions on the thermal transition of ribonuclease. J Phys Chem 69:298-303.
43. Schrier EE, Mackey LD. 1968. The effect of salt of organic acids and bases on the thermal transition of ribonuclease. J Phys Chem 72:733-736.
44. Scott RA, Scheraga HA. 1963. Structural studies of ribonuclease. XI. Kinetics of denaturation. J Am Chem Soc 85:3866-3873.
45. Shirley BA, Stanssens P, Hahn V, Pace CN. 1992. Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. Biochemistry 31:725-732.
46. Sosnick TR, Trewhella J. 1992. Denatured states of ribonuclease A have compact dimensions and residual secondary structure. Biochemistry 31:8329-8335.
47. Stokes RH. 1967. Thermodynamics of aqueous urea solutions. Aust J Chem 20:2087-2100.
48. Tsong TYT, Hearn RP, Wrathall DP, Sturtevant JM. 1970. A calorimetric study of thermally induced conformational transitions of ribonuclease A and certain of its derivatives. Biochemistry 9:2666-2677.
49. Xie G, Timasheff SN. 1997a. Mechanism of the stabilization of ribonuclease A by sorbitol: Preferential hydration is greater for the denatured than for the native protein. Protein Sci 6:211-221.
50. Xie G, Timasheff SN. 1997b. Temperature dependence of the preferential interactions of ribonuclease A in aqueous co-solvent systems: Thermodynamic analysis. Protein Sci 6:222-232.
51. von Hippel PH, Wong KY. 1965. The conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition. J Biol Chem 240:3909-3923.