The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
HEAT CAPACITY IN PROTEINS
Abstract
▪ Abstract Heat capacity (Cp) is one of several major thermodynamic quantities commonly measured in proteins. With more than half a dozen definitions, it is the hardest of these quantities to understand in physical terms, but the richest in insight. There are many ramifications of observed Cp changes: The sign distinguishes apolar from polar solvation. It imparts a temperature (T) dependence to entropy and enthalpy that may change their signs and which of them dominate. Protein unfolding usually has a positive ΔCp, producing a maximum in stability and sometimes cold denaturation. There are two heat capacity contributions, from hydration and protein-protein interactions; which dominates in folding and binding is an open question. Theoretical work to date has dealt mostly with the hydration term and can account, at least semiquantitatively, for the major Cp-related features: the positive and negative Cp of hydration for apolar and polar groups, respectively; the convergence of apolar group hydration entropy at T ≈ 112°C; the decrease in apolar hydration Cp with increasing T; and the T-maximum in protein stability and cold denaturation.
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Cites
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Cited by
Snyder, P. W., Mecinović, J., Moustakas, D. T., Thomas, S. W., Harder, M., Mack, E. T., Lockett, M. R., Héroux, A., Sherman, W., & Whitesides, G. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114107108 · Cited by 357
Rigidity versus flexibility: the dilemma of understanding protein thermal stability
Karshikoff, A., Nilsson, L., & Ladenstein, R. (2015) · The FEBS Journal · doi:10.1111/febs.13343 · Cited by 281
Assembly and solution structure of the core retromer protein complex
Norwood, S. J., Shaw, D. J., Cowieson, N. P., Owen, D. J., Teasdale, R. D., & Collins, B. M. (2011) · Traffic · doi:10.1111/j.1600-0854.2010.01124.x · Cited by 84
Role of Ordered Proteins in the Folding-Upon-Binding of Intrinsically Disordered Proteins
Lawrence, C. W., Kumar, S., Noid, W. G., & Showalter, S. A. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz402729x · Cited by 25
Differential scanning calorimetry of native silk feedstock
Holland, C., Hawkins, N., Frydrych, M., Laity, P., Porter, D., & Vollrath, F. (2019) · Macromolecular Bioscience · doi:10.1002/mabi.201800228 · Cited by 18
Metadata
- Authors
- Prabhu, N. V., & Sharp, K. A.
- Venue
- Annual Review of Physical Chemistry
- Publisher
- Annual Reviews
- Published
- 2005-05-05
- Volume
- 56
- Issue
- 1
- Pages
- 521-548
- ISSN
- 0066-426X (ISSN-L)
- 1545-1593
- OpenAlex
- W2125039552
- Cited by
- 425
- References
- 52
- FWCI
- 1.28
- Type
- journal article
- Language
- en
- Open access
- closed
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