Heat capacity change for ribonuclease A folding

Protein Science

Volumn 8, Issue 7, 1999, Pages 1500-1504

  Pace, C Nick ^a   Grimsley, Gerald R ^a   Thomas, Susan T ^b   Makhatadze, George I ^b  

^a TEXAS A AND M UNIVERSITY   (United States)

^b TEXAS TECH UNIVERSITY   (United States)

Author keywords

Differential scanning calorimetry; Heat capacity change; Protein folding; Protein stability; Ribonuclease A; Urea denaturation

Indexed keywords

RIBONUCLEASE A;

ARTICLE; CALCULATION; CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVITY; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE; THERMOSTABILITY;

EID: 0032776418     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.7.1500     Document Type: Article

References (46)

1. Allen DL, Pielak GJ. 1998. Baseline length and automated fitting of denaturation data. Protein Sci 7:1262-1263.
2. Arnold U, Ulbrich-Hofmann R. 1997. Kinetic and thermodynamic thermal stabilities of ribonuclease A and ribonuclease B. Biochemistry 36:2166-2172.
3. Barone G, Del Vecchio P, Ressas D, Giancola C, Graziano G, Riccio A. 1994. Thermodynamic characterisation of RNase A in the presence of urea and GuHCl. J Thermal Anal 41:1357-1370.
4. Baskakov IV, Bolen DW. 1998. Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: Implications regarding m values, intermediates, and thermodynamics. Biochemistry 37:18010-18017.
5. Becktel WJ, Schellman JA. 1987. Protein stability curves. Biopolymers 26:1859-1877.
6. Brandts JF, Hunt L. 1967. The thermodynamics of protein denaturation. III. The denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixtures. J Am Chem Soc 89:4826-4838.
7. Carra JH, Anderson EA, Privalov PL. 1994. Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. Biochemistry 33:10842-10850.
8. Catanzano F, Graziano G, Capasso S, Barone G. 1997. Thermodynamic analysis of the effect of selective monodeamidation at asparagine 67 in ribonuclease A. Protein Sci 6:1682-1693.
9. Chiti F, van Nuland NA-J, Taddei N, Magherini F, Stefani M, Ramponi G, Dobson CM. 1998. Conformational stability of muscle acylphosphatase: The role of temperature, denaturant concentration, and pH. Biochemistry 37:1447-1455.
10. Foss JG, Schellman JA. 1959. The thermal transition of ribonuclease in urea solutions. J Am Chem Soc 63:2007-2012.
11. Freire E, Biltonen RL. 1978. Statistical mechanical deconvolution of thermal transitions in macromolecules I. Theory and application to homogeneous systems. Biopolymers 17:463-479.
12. 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.
13. Grantcharova VP, Baker D. 1997. Folding dynamics of the src SH3 domain. Biochemistry 36:15685-15692.
14. Greene RF, Pace CN. 1974. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymostypsin, and β-lactoglobulin. J Biol Chem 249:5388-5393.
15. Griko YV, Freire E, Privalov PL. 1994. Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 33:1889-1899.
16. Griko YV, Privalov PL. 1992. Calorimetric study of the heat and cold denaturation of β-lactoglobulin. Biochemistry 31:8810-8815.
17. Griko YV, Privalov PL. 1994. Thermodynamic puzzle of apomyoglobin unfolding. J Mol Biol 235:1318-1325.
18. Hawley SA. 1971. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10:2436-2442.
19. Hinz H-J, Vogl T, Meyer R. 1994. An alternative interpretation of the heat capacity changes associated with protein unfolding. Biophys Chem 52:275-285.
20. Jackson WM, Brandts JF. 1970. Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation. Biochemistry 9:2294-2301.
21. p, and evaluation of solvent isotope effects. Protein Sci 7:2405-2412.
22. 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.
23. Makhatadze GI. 1998. Measuring protein thermostability by differential scanning calorimetry. Curr Prot Pro Sci 12:7.9.1-7.9.14.
24. Makhatadze GI, Clore GM, Groneborn AM. 1995. Solvent isotope effect and protein stability. Nature Struct Biol 2:852-855.
25. Makhatadze GI, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride. A calorimetric study. J Mol Biol 226:491-505.
26. Makhatadze GI, Privalov PL. 1995. Energetics of protein structure. Adv Protein Chem 47:307-425.
27. McCrary BS, Bedell J, Edmonson SP, Shriver JW. 1998. Linkage of protonation and anion binding to the folding of Sac7d. J Mol Biol 276:203-224.
28. Myers JK, Pace CN, Scholtz JM. 1995. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci 4:2138-2148.
29. Nicholson EM, Scholtz JM. 1996. Conformational stability of the Escherichia coli HPr protein: Test of the linear extrapolation method and a thermodynamic characterization of cold denaturation. Biochemistry 35:11369-11378.
30. Pace CN. 1990. Measuring and increasing protein stability. TIBTECH 8:93-98.
31. Pace CN, Hebert EJ, Shaw KL, Schell D, Both V, Krajcikova D, Sevcik J, Wilson KS, Dauter Z, Hartley RW, Grimsley GR. 1998. Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2, and Sa3. J Mol Biol 279:271-286.
32. Pace CN, Laurents DV. 1989. A new method for determining the heat capacity change for protein folding. Biochemistry 28:2520-2525.
33. Pace CN, Laurents DV, Thomson JA. 1990. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry 29:2564-2572.
34. Pace CN, Tanford C. 1968. Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 5.5. Biochemistry 1:198-208.
35. Pfeil W. 1998. Protein stability and folding: A collection of thermodynamic data. Berlin Heidelberg: Springer-Verlag.
36. Pfeil W, Privalov PL. 1976. Thermodynamic investigations of proteins. I. Standard functions for proteins with lysozyme as an example. Biophys Chem 4:23-32.
37. Plotnikov VV, Brandts JM, Lin L-N, Brandts JF. 1997. A new ultrasensitive scanning calorimeter. Anal Biochem 250:237-244.
38. Privalov PL. 1990. Cold denaturation of proteins. Crit Rev Biochem Mol Biol 25:281-305.
39. Privalov PL, Tiktopulo EI, Khechinashvili NN. 1973. Calorimetric investigation of ribonuclease thermal denaturation. Int J Pept Protein Res 5:229-237.
40. Salahuddin A, Tanford C. 1970. Thermodynamics of the denaturation of ribonuclease by guanidine hydrochloride. Biochemistry 9:1342-1347.
41. Scholtz JM. 1995. Conformational stability of HPr: The histidine-containing phosphocarrier protein from Bacillus subtilis. Protein Sci 4:35-43.
42. Schwarz FP, Kirchhoff WH. 1988. Biological thermodynamic data for the calibration of differential scanning calorimeters: Heat capacity data on the unfolding transition of ribonuclease A in solution. Thermochim Acta 128:267-295.
43. Shiao DF. Lumry R, Fahey J. 1971. Studies of the chymotrypsinogen family of proteins. XI. Heat-capacity changes accompanying reversible thermal unfolding of proteins. J Am Chem Soc 93:2024-2035.
44. Tanford C. 1968. Protein denaturation. Adv Protein Chem 23:121-282.
45. Yamaguchi T, Yamada H, Akasaka K. 1995. Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR. J Mol Biol 250:689-694.
46. Yao M, Bolen DW. 1995. How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry 34:3771-3781.