Crossref journal-article
Wiley
Protein Science (311)
Abstract

AbstractAbsorbance‐detected thermal denaturation studies of the C102T variant of Saccharomyces cerevisiae iso‐1‐ferricytochrome c were performed between pH 3 and 5. Thermal denaturation in this pH range is reversible, shows no concentration dependence, and is consistent with a 2‐state model. Values for free energy (ΔGD), enthalpy (ΔHD), and entropy (ΔSD) of denaturation were determined as functions of pH and temperature. The value of ΔGD at 300 K, pH 4.6, is 5.1 ± 0.3 kcal mol−1. The change in molar heat capacity upon denaturation (ΔCp), determined by the temperature dependence of ΔHD as a function of pH (1.37 ± 0.06 kcal mol−1 K−1), agrees with the value determined by differential scanning calorimetry. pH‐dependent changes in the Soret region indicate that a group or groups in the heme environment of the denatured protein, probably 1 or both heme propionates, ionize with a pK near 4. The C102T variant exhibits both enthalpy and entropy convergence with a ΔHD of 1.30 kcal mol−1 residue−1 at 373.6 K and a ΔSD of 4.24 cal mol−1 K−1 residue−1 at 385.2 K. These values agree with those for other single‐domain, globular proteins.

Bibliography

Cohen, D. S., & Pielak, G. J. (1994). Stability of yeast iso‐1‐ferricytochrome c as a function of pH and temperature. Protein Science, 3(8), 1253–1260. Portico.

Authors 2
  1. David S. Cohen (first)
  2. Gary J. Pielak (additional)
References 49 Referenced 64
  1. 10.1126/science.181.4096.223
  2. 10.1021/bi00099a028
  3. 10.1002/pro.5560021218
  4. 10.1073/pnas.83.21.8069
  5. 10.1002/bip.360261104
  6. 10.1016/0022-2836(92)90255-I
  7. 10.1021/bi00164a007
  8. 10.1016/0959-440X(93)90090-8
  9. 10.1021/ja00043a062
  10. 10.1016/S0959-440X(05)80118-6
  11. 10.1016/S0021-9258(20)79752-8 / J Biol Chem / Nuclear magnetic resonance titration curves of histidine ring protons by Cohen JS (1974)
  12. 10.1093/protein/1.2.95
  13. 10.1021/bi00483a001
  14. 10.1146/annurev.bi.60.070191.004051
  15. 10.1021/bi00154a007
  16. 10.1016/S0021-9258(19)39863-1 / J Biol Chem / Differential stability of two apo‐isocytochromes c in the yeast Saccharomyces cerevisiae by Dumont MD (1990)
  17. {'key': 'e_1_2_1_18_1', 'first-page': '452', 'volume-title': 'Biophysical chemistry', 'author': 'Edsall JT', 'year': '1958'} / Biophysical chemistry by Edsall JT (1958)
  18. 10.1016/0005-2795(77)90166-0
  19. 10.1021/bi00054a026
  20. 10.1073/pnas.89.19.9335
  21. 10.1021/bi00221a028
  22. 10.1021/bi00482a007
  23. 10.1016/0162-0134(93)85038-A
  24. 10.1042/bj2580595 / Biochem J / A denaturation‐induced proton‐uptake study of horse cytochrome c by Hartshorn RT (1988)
  25. 10.1021/ja00086a046
  26. 10.1021/ja01476a025
  27. 10.1016/0162-0134(93)85036-8
  28. 10.1016/S0021-9258(18)48213-0 / J Biol Chem / Replacement of the invariant lysine 77 by arginine in yeast iso‐1‐cytochrome c results in enhanced and normal activities in vitro and in vivo by Holzschu D (1987)
  29. 10.1016/S0021-9258(19)46967-6 / J Biol Chem / Mutagenesis at a specific position in a DNA sequence by Hutchinson CA (1978)
  30. 10.1016/S0065-3233(08)60608-7
  31. 10.1042/bj2990347 / Biochem J / The significance of denaturant titrations of protein stability: A comparison of rat and baker's yeast cytochrome c and their site‐directed asparagine‐52‐to‐isoleucine mutants by Koshy TI (1994)
  32. 10.1002/bip.1966.360040808
  33. 10.1002/pro.5560021204
  34. {'key': 'e_1_2_1_35_1', 'first-page': '1966', 'article-title': 'Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso‐1‐cytochrome c Protein', 'volume': '2', 'author': 'Marmorino JL', 'year': '1993', 'journal-title': 'Sci'} / Sci / Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso‐1‐cytochrome c Protein by Marmorino JL (1993)
  35. 10.1007/978-3-642-74536-2
  36. 10.1016/0022-2836(91)90506-2
  37. 10.1016/B978-0-12-058757-5.50060-3
  38. {'key': 'e_1_2_1_39_1', 'first-page': '311', 'volume-title': 'Protein structure: A practical approach', 'author': 'Pace CN', 'year': '1990'} / Protein structure: A practical approach by Pace CN (1990)
  39. 10.1007/978-3-642-72698-9
  40. 10.1016/0301-4622(76)80005-1
  41. 10.1016/B978-1-4831-9718-0.50010-2
  42. 10.1016/S0065-3233(08)60377-0
  43. 10.1016/0022-2836(74)90188-0
  44. 10.1006/jmbi.1993.1417
  45. 10.1002/bip.1969.360080502
  46. 10.1002/bip.1969.360070402
  47. 10.1016/0092-8674(79)90091-6
  48. 10.1021/bi00388a026
  49. 10.1021/bi00080a025
Dates
Type When
Created 16 years, 6 months ago (Feb. 9, 2009, 9 p.m.)
Deposited 1 year, 10 months ago (Oct. 24, 2023, 2:17 a.m.)
Indexed 1 month, 3 weeks ago (July 4, 2025, 7:48 a.m.)
Issued 31 years ago (Aug. 1, 1994)
Published 31 years ago (Aug. 1, 1994)
Published Online 16 years, 7 months ago (Dec. 31, 2008)
Published Print 31 years ago (Aug. 1, 1994)
Funders 0

None

@article{Cohen_1994, title={Stability of yeast iso‐1‐ferricytochrome c as a function of pH and temperature}, volume={3}, ISSN={1469-896X}, url={http://dx.doi.org/10.1002/pro.5560030811}, DOI={10.1002/pro.5560030811}, number={8}, journal={Protein Science}, publisher={Wiley}, author={Cohen, David S. and Pielak, Gary J.}, year={1994}, month=aug, pages={1253–1260} }