| Proc Natl Acad Sci U S A. 1977 June; 74(6): 2236–2240. | PMCID: PMC432144 |
Heat capacity and entropy changes in processes involving proteins. J M Sturtevant Abstract Six possible sources of the large heat capacity and entropy changes frequently observed for processes involving proteins are identified. Of these the conformational, hydrophobic, and vibrational effects seem likely to be of greatest importance. A method is proposed for estimating the magnitudes of the hydrophobic and vibrational contributions. Application of this method to several protein processes appears to achieve significant clarification of previously confusing and apparently contradictory data. Full text Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (897K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References. These references are in PubMed. This may not be the complete list of references from this article. - Niekamp, CW; Sturtevant, JM; Velick, SF. Energetics of the cooperative and noncooperative binding of nicotinamide adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase at pH 6.5 and pH 8.5. Equilibrium and calorimetric analysis over a range of temperature. Biochemistry. 1977 Feb 8;16(3):436–445. [PubMed]
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- Schmid, F; Hinz, HJ; Jaenicke, R. Thermodynamic studies of binary and ternary complexes of pig heart lactate dehydrogenase. Biochemistry. 1976 Jul 13;15(14):3052–3059. [PubMed]
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- Hinz, HJ; Weber, K; Flossdorf, J; Kula, MR. Thermodynamic studies on the specificity of L-isoleucine-tRNA ligase of Escherichia coli MRE 600. Calorimetric investigations on binding of amino acids and isoleucinol to the enzyme. Eur J Biochem. 1976 Dec 11;71(2):437–442. [PubMed]
- Suurkuusk, J; Wadsö, I. Thermochemistry of the avidin-biotin reaction. Eur J Biochem. 1972 Jul 24;28(3):438–441. [PubMed]
- Hearn, RP; Richards, FM; Sturtevant, JM; Watt, GD. Thermodynamics of the binding of S-peptide to S-protein to form ribonuclease S.. Biochemistry. 1971 Mar 2;10(5):806–817. [PubMed]
- Lavialle, F; Rogard, M; Alfsen, A. Calorimetric determination of the enthalpy and heat capacity changes for the association of haptoglobin with hemoglobin. I. Demonstration of two interacting systems. Biochemistry. 1974 May 7;13(10):2231–2234. [PubMed]
- Barisas, BG; Singer, SJ; Sturtevant, JM. Thermodynamics of the binding of 2,4-dinitrophenyl and 2,4,6-trinitrophenyl haptens to the homologous and heterologous rabbit antibodies. Biochemistry. 1972 Jul 18;11(15):2741–2744. [PubMed]
- Johnston, MF; Barisas, BG; Sturtevant, JM. Thermodynamics of hapten binding to MOPC 315 and MOPC 460 mouse myeloma proteins. Biochemistry. 1974 Jan 15;13(2):390–396. [PubMed]
- Jackson, WM; Brandts, JF. Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation. Biochemistry. 1970 May 26;9(11):2294–2301. [PubMed]
- Privalov, PL; Khechinashvili, NN; Atanasov, BP. Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of chymotrypsinogen, ribonuclease and myoglobin. Biopolymers. 1971 Oct;10(10):1865–1890. [PubMed]
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- Tsong, TY; Hearn, RP; Wrathall, DP; Sturtevant, JM. A calorimetric study of thermally induced conformational transitions of ribonuclease A and certain of its derivatives. Biochemistry. 1970 Jun 23;9(13):2666–2677. [PubMed]
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- Shiao, DD; Sturtevant, JM. Heats of thermally induced helix-coil transitions of DNA in aqueous solution. Biopolymers. 1973;12(8):1829–1836. [PubMed]
- Privalov, PL; Filimonov, VV; Venkstern, TV; Bayev, AA. A calorimetric investigation of tRNAVal1 melting. J Mol Biol. 1975 Sep 25;97(3):279–288. [PubMed]
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- Durchschlag, H; Puchwein, G; Kratky, O; Schuster, I; Kirschner, K. X-ray small-angle scattering of yeast glyceraldehyde-3-phosphate dehydrogenase as a function of saturation with nicotinamide-adenine-dinucleotide. Eur J Biochem. 1971 Mar 1;19(1):9–22. [PubMed]
- Chothia, C. Structural invariants in protein folding. Nature. 1975 Mar 27;254(5498):304–308. [PubMed]
- Nozaki, Y; Tanford, C. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J Biol Chem. 1971 Apr 10;246(7):2211–2217. [PubMed]
- Brandts, JF; Oliveira, RJ; Westort, C. Thermodynamics of protein denaturation. Effect of pressu on the denaturation of ribonuclease A. Biochemistry. 1970 Feb 17;9(4):1038–1047. [PubMed]
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