DOI: 10.1002/prot.340220410. The heat capacity of proteins

10.1002/prot.340220410

Crossref journal-article

Wiley

Proteins: Structure, Function, and Bioinformatics (311)

Abstract

AbstractThe heat capacity plays a major role in the determination of the energetics of protein folding and molecular recognition. As such, a better understanding of this thermodynamic parameter and its structural origin will provide new insights for the development of better molecular design strategies. In this paper we have analyzed the absolute heat capacity of proteins in different conformations. The results of these studies indicate that three major terms account for the absolute heat capacity of a protein: (1) one term that depends only on the primary or covalent structure of a protein and contains contributions from vibrational frequencies arising from the stretching and bending modes of each valence bond and internal rotations; (2) a term that contains the contributions of noncovalent interactions arising from secondary and tertiary structure; and (3) a term that contains the contributions of hydration. For a typical globular protein in solution the bulk of the heat capacity at 25°C is given by the covalent structure term (close to 85% of the total). The hydration term contributes about 15 and 40% to the total heat capacity of the native and unfolded states, respectively. The contribution of non‐covalent structure to the total heat capacity of the native state is positive but very small and does not amount to more than 3% at 25°C. The change in heat capacity upon unfolding is primarily given by the increase in the hydration term (about 95%) and to a much lesser extent by the loss of noncovalent interactions (up to ∼5%). It is demonstrated that a single universal mathematical function can be used to represent the partial molar heat capacity of the native and unfolded states of proteins in solution. This function can be experimentally written in terms of the molecular weight, the polar and apolar solvent accessible surface areas, and the total area buried from the solvent. This unique function accurately predicts the different magnitude and temperature dependences of the heat capacity of both the native and unfolded states, and therefore of the heat capacity changes associated with folding/unfolding transitions. © 1995 Wiley‐Liss, Inc.

Bibliography

GÃ³mez, J., Hilser, V. J., Xie, D., & Freire, E. (1995). The heat capacity of proteins. Proteins: Structure, Function, and Bioinformatics, 22(4), 404â412. Portico.

Authors 4

Javier Gómez (first)
Vincent J. Hilser (additional)
Dong Xie (additional)
Ernesto Freire (additional)

References 28 Referenced 382

10.1016/0022-2836(74)90188-0
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10.1016/0022-2836(92)90555-X
10.1016/0022-2836(92)90699-K
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10.1002/prot.340190404
10.1016/S0022-2836(05)80198-6
10.1002/pro.5560030414
10.1002/pro.5560021204
10.1021/bi00197a037
10.1021/bi00173a036
10.1002/pro.5560031203
{'key': 'e_1_2_1_14_2', 'volume-title': 'Thermochemical Kinetics', 'author': 'Benson S. W.', 'year': '1968'} / Thermochemical Kinetics by Benson S. W. (1968)
10.1002/bip.360320303
10.3891/acta.chem.scand.28b-0409
10.1021/bi00579a035
{'key': 'e_1_2_1_18_2', 'volume-title': 'Estimation of Thermodynamic Properties of Organic Compounds', 'author': 'Janz G. J.', 'year': '1958'} / Estimation of Thermodynamic Properties of Organic Compounds by Janz G. J. (1958)
10.1021/ja00838a005
{'key': 'e_1_2_1_20_2', 'volume-title': 'Handbook of Chemistry and Selected Data for Molecular Biology', 'author': 'Hutchens J. O.', 'year': '1970'} / Handbook of Chemistry and Selected Data for Molecular Biology by Hutchens J. O. (1970)
10.1063/1.1744539
10.1016/S0021-9258(19)78185-X / J. Biol. Chem. / Heat capacities from 11 to 305 K and entropies of hydrated and anhydrous bovine zinc insulin and bovine chymotrypsinogen A by Hutchens J. O. (1969)
10.1021/bi00285a025
10.1021/bi00179a018
10.1006/jmbi.1994.1430
10.1006/jmbi.1994.1557
10.1021/bi00177a023
10.1002/prot.340180305
10.1016/0022-2836(71)90324-X

Dates

Type	When
Created	20 years, 2 months ago (May 28, 2005, 9:42 p.m.)
Deposited	1 year, 9 months ago (Oct. 25, 2023, 8:20 p.m.)
Indexed	3 weeks ago (Aug. 2, 2025, 12:29 a.m.)
Issued	30 years ago (Aug. 1, 1995)
Published	30 years ago (Aug. 1, 1995)
Published Online	21 years, 6 months ago (Feb. 3, 2004)
Published Print	30 years ago (Aug. 1, 1995)

Funders 0

None

BibTeX

@article{G_mez_1995, title={The heat capacity of proteins}, volume={22}, ISSN={1097-0134}, url={http://dx.doi.org/10.1002/prot.340220410}, DOI={10.1002/prot.340220410}, number={4}, journal={Proteins: Structure, Function, and Bioinformatics}, publisher={Wiley}, author={Gómez, Javier and Hilser, Vincent J. and Xie, Dong and Freire, Ernesto}, year={1995}, month=aug, pages={404–412} }

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