Van't Hoff enthalpies without baselines

Protein Science

Volumn 9, Issue 7, 2000, Pages 1416-1419

  John, Deborah M ^a   Weeks, Kevin M ^a  

^a University of North Carolina at Chapel Hill   (United States)

Author keywords

Analysis of protein denaturation; Differential melting curve; Van't Hoff enthalpy

Indexed keywords

ARTICLE; CALCULATION; ENTHALPY; MATHEMATICAL ANALYSIS; MELTING POINT; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STABILITY; TEMPERATURE;

EID: 0033858359     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.7.1416     Document Type: Article

References (16)

1. Allen DL, Pielak GJ. 1998. Baseline length and automated fitting of denaturation data. Protein Sci 7:1262-1263.
2. Cooper A. 1999. Thermodynamic analysis of biomolecular interactions. Curr Opin Chem Biol 3:557-563.
3. Elwell M, Schellman J. 1975. Phage T4 lysozyme. Physical properties and reversible unfolding. Biochim Biophys Acta 386:309-323.
4. Eriksson AE, Baase WA, Zhang X-J, Heinz DW, Blaber M, Baldwin EP, Mathews BW. 1992. Response of a protein structure to cavity creating mutations and its relation to the hydrophobic effect. Science 255:178-183.
5. Fersht A. 1999. Structure and mechanism in protein science. New York: W.H. Freeman and Co. pp 508-539, 547-553.
6. Freire E. 1995. Thermal denaturation methods in the study of protein folding. Methods Enzymol 259:144-168.
7. Gralla J, Crothers DM. 1973. Free energy of imperfect nucleic acid helices. J Mol Biol 78:301-319.
8. Hermans J. 1965. Methods for the study of reversible denaturation of proteins and interpretation of data. Methods Biochem Anal 13:81-111.
9. Hickey DR, Berghuis AM, Lafond G, Jaeger JA, Cardillo TS, McLendon D, Das G, Sherman F, Brayer GD, McLendon G. 1991. Enhanced thermodynamic stabilities of yeast iso-1-cytochromes c with amino acid replacements at positions 52 and 102. J Biol Chem 266:11686-11694.
10. Hostetter DR, Weatherly GT, Beasley JR, Bortone K, Cohen DS, Finger SA, Hardwidge P, Kakouras DS, Saunders AJ, Trojak SK, Waldner JC, Pielak GJ. 1999. Partially formed native tertiary interactions in the A-state of cytochrome c. J Mol Biol 289:639-644.
11. John DM, Weeks KM. 2000. Tagging DNA mismatches by selective 2′-amine acylation. Chem Biol 7:405-410.
12. Kauzmann W. 1959. Some factors in the interpretation of protein denaturation. Adv Protein Chem 14:1-63.
13. Lumry R, Bioltonen R, Brandts JF. 1966. Validity of the "two-state" hypothesis for conformational transitions of proteins. Biopolymers 4:917-944.
14. Marky LA, Breslauer KJ. 1987. Calculating thermodynamic data for transition of any molecularity from equilibrium melting curves. Biopolymers 26:1601-1620.
15. Marmorino JL, Lehti M, Pielak GJ. 1997. Native tertiary structure in an A-state. J Mol Biol 275:379-388.
16. Marmorino JL, Pielak GJ. 1995. A native tertiary interaction stabilizes the A-state of cytochrome c. Biochemistry 34:3140-3143.