Thermodynamics of Unfolding of the All .beta.-Sheet Protein Interleukin-1.beta
| Autor: | G M Clore, Privalov Pl, Angela M. Gronenborn, George I. Makhatadze |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
chemistry.chemical_classification
Protein Denaturation Calorimetry Differential Scanning Globular protein Beta sheet Thermodynamics Hydrogen Bonding Models Theoretical Biochemistry Heat capacity Protein Structure Secondary Recombinant Proteins Gibbs free energy Hydrophobic effect symbols.namesake Differential scanning calorimetry chemistry Escherichia coli symbols Humans Denaturation (biochemistry) Cloning Molecular Beta (finance) Mathematics Interleukin-1 |
| Zdroj: | Biochemistry. 33:9327-9332 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi00197a037 |
| Popis: | The thermal denaturation of interleukin-1 beta in solution has been studied by differential scanning calorimetry at various pH values. It is shown that the thermal transition of interleukin-1 beta is completely reversible below pH 2.5, only partly reversible in the pH range 2.5-3.5, and irreversible above pH 3.5. Analysis of the reversible unfolding of interleukin-1 beta shows that the heat denaturation is well approximated by a two-state transition and is accompanied by a significant increase of heat capacity. The partial heat capacity of denatured interleukin-1 beta is very close to that expected for the completely unfolded protein. This permitted us to assign the thermodynamic characteristics of interleukin-1 beta denaturation to its complete unfolding and to correlate them with structural features of the protein. The contributions of hydrogen bonding and hydrophobic interactions to the stability of interleukin-1 beta are analyzed and compared to those for other globular proteins. It is shown that the Gibbs energy of a hydrogen bond in a beta-sheet structure is greater than in alpha-helices. |
| Databáze: | OpenAIRE |
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